Post by Dr. Hildegarde Staninger on Sept 2, 2007 18:23:45 GMT -5
(Continued from PART I)
Copyright © 2009 Dr. Hildegarde Staninger, RIET-1
Industrial Toxicologist/IH,
Doctor of Integrative Medicine
Integrative Health Systems, LLC
415 3/4th N. Larchmont Blvd.,
Los Angeles, CA 90004
Tel: 323-466-2599 Fax: 323-466-2774
www.hildegarde-staninger.com
www.healinggrapevine.com
The Future of Superoxid Dismutases and Nutritional Modulation
NASA principal investigator, Dr. Gloria Borgstahl, formerly of the University of Toledo, and now of the University of Nebaraska, has successfully crystallized E. coli manganese superoxide dismutase (MnSOD), antioxidant enzymes that are homologous to those found in cellular mitochondria, on the International Space Station during the period of December 2001 to April 2002. Several of the MnSOD crystals grown on ISS were 80 times greater in crystal volume than earth-grown crystals. Di spots to 1.26 resolutions were observed providing significantly improved data obtained from crystals grown in earth laboratories. An exciting result was that the MnSOD crystals grown on ISS were suitable for neutron studies and time-Laue studies-methods that require large, perfect crystals. With the neutron examples the researchers hope to be able to obtain the, never-before-seen, three-dimensional structure of the hydrogen’s on each amino acid of the protein and thereby be able to answer the unsolved questions concerning the source of these hydrogens in this reaction mechanism. With the time-resolved Laue experiments, the team will be able to generate the superoxide substrate within the crystals with a laser pulse and thus film the “movie” of the enzyme converting it to the products peroxide and water. The enzyme MnSODs in the body is important, and in-depth study of their structure is not to the ability to understand their true function, but these experiments may lead to new therapeutics for the treatment of various degenerative diseases.18
Superoxide dismutases (SODs) are antioxidant metalloenzymes catalyzing the redox disproportion in the (dismutation) of superoxide radical, O2*- as previously discussed in Equation (1).
It is generally accepted that in all SODs the metal ion (M) catalyzes dismutation of the superoxide radical through a cyclic oxidation reduction mechanism:
M3+ + O2*- --> M2+ + O2 (1.1)
M2+ + O2*- + 2H+ ---> M3+ + H2O2 (1.2)
The four classes of SODs are known, distinguished by the metal prosthetic groups: Cu/Zn, FE, Mn and Ni. Fe- and Mn- SODs constitute a structural family.26,27 Fe- and Mn- SODs are unequally distributed throughout the kingdoms of living organisms and are located in different cellular compartments.28,29,30,31 In particular, Fe-SOD is found in obligate anaerobes and aerobic diazotrophs (exclusively), facultative aerobes (exclusively or together with Mn-SOD). In the cytosol of cyanobacteria, in the chloroplast stroma of higher plants, in the protozoa, kelp, Yamatoshinjo and Oaky Smoky (Cu/Zn-SOD, Fe-SOD, Mn-SOD)TM 32,33,34 Fe-SOD and Mn-SOD form some organisms (e.g. Escherichia coli ) exhibit almost absolute metal specificity ,35 while other enzymes, such as “cambialistic” SOD form Propionibacterium shermanii, are captive with either metal.36 Fe- and Mn-SODs occur as homodimers or homotetramiers.
The 3-D structures of several Fe-SODs have been determined. 36,37,38,39,40 The monomers fold into two domains. The N-terminal domain consists of two long antiparallel helices. The C-terminal domain contains a central beta-sheet formed by three antiparallel beta strands with 4-6 surrounding helices. The iron atom is lignaded by two residues from each of the N-terminal helices and two residues from the loops in the C-terminal domain.
The active site iron is pentacoordinate, with the metal lignands (N x epsilon) of three conserved His residues, O x delta of the conserved Asp residue of a water molecule) arranged in distorted trigonal bipyramidal geometry, which opposite of the tetrahydronal molecule of water. The first His residue and a solvent molecule fill the two axial positions. In the azide-FeIII –SOD complex, the iron becomes hexacoodinate with distorted octahedral geometry (similar to the fat soluble Vitamin E), with azide coordinated trans to ASP ligand.41 Table 1 lists the mononuclear iron environment residues in known 3D structures with their PDB Code and Reference.
Superoxide dismutases (SODs) have been found in various nutritional sources such as Jerusalem artichoke powder and Bifidobacterium. 42,43 Juice Plus + Vineyard Blend, foods grown in red clay soils, Yamatoshinjo and hemp oil. 44, 34,45 The use of these nutritional modulators have shown significant risk to oxidative stress via the superoxide radical as they have maintained cellular integrity and reduced cellular sensitization as individual whole foods with an individual’s meals.
Summary
Cells are continuously exposed to a variety of oxidative process which could potentially lead to cellular injury or death. As a result, aerobic organisms possess effective defense mechanisms against oxidative stress as associated with the superoxide radical and improper nutritional modulation that would reduce superoxide dismutases (SODs) in the cell and thereby circumvent toxic cell injury. These protective mechanisms fall into two broad categories: (1) those which prevent the initiation of lipid peroxidation and (2) those which prevent its propagation.
Superoxide dismutase and catalase provide antioxidant protection by inhibiting the formation of the hydroxyl radical. Chelation of the ferric iron necessary for the formation of the hydroxyl radical and direct removal of this species by radical scavengers (e.g., mannital) are also protective. The generation of species capable of initiating peroxidation may exceed the capacity of effectively remove them. Thus, there are other defenses to prevent the uncontrolled propagation of lipid peroxidation and oxidative stress as associated with free oxygen radicals/hydroxyl radicals. These include water-soluble antioxidants, such as ascorbic acid (vitamin C) and reduced glutathione, and fat-soluble antioxidants, most notably alpha-tocopherol (vitamin E). It appears that vitamins E and C and glutathione combine in some as yet poorly defined cycle to donate hydrogen atoms to lipid and/or peroxy radicals, thereby preventing further propagation of the lipid peroxidation, which was initiated by free oxygen radicals.
The metabolism of toxic substances as associated with hazardous materials by mixed function oxidation or other mechanisms leads to irreversible cell injury thorough mechanisms that have been related either to the covalent binding of reactive metabolites, to changes in protein thiols, to alterations in intracellular calcium homeostasis, or to the formation of partially reduced oxygen species. The relative roles that each of these mechanisms plays in any particular example of toxic cell injury remains controversial and a subject of continuing investigation through the advancement of new analytical technologies/equipment. In the case of the various forms of superoxide dismutases, “quickened” advances in science, chemistry and wave genetics 46 will show that these metalloenzymes will play a major character role in the explanation of “creation” through the variable of true far infrared sources, superluminal radiance, the effects of Cooper pairs upon EcceleratedTM intelligent water and the role of the white worm hole found in black holes as recently found in the DNA molecule. These future researchers will be the Indigo and Crystal children – our grand children with their little pet black rabbit with pink ears and a white spot named Ben as it hops down a white worm hole in the quantum biophysics of the human cell. Time and Eternity will show all of us the wonders that will amaze the original Creator of us all through the marvels of science, spirituality, art and medicine.
References
1 U.S. Department of Health, Education, and Welfare. Occupational Diseases: A Guide to Their Recognition. U.S. Government Printing Office, Washington, D.C. Revised Edition June 1977 pgs. 31-41.
2 Kyle, Marlene E. and John L. Farber. Handbook of Toxicologic Pathology. Chapter 6: Biochemical Mechanisms of Toxic Cell Injury. Academic Press, Inc. New York © 1991.
3 Goldberg, Burton. Alternative Medicine Guide to Cancer. Future Medicine, Inc., Tiberon, CA.
pgs, 731-736 Maverick Test by Dr. Hildegarde Staninger. © 1996
4 Staninger, Hildegarde. Maverick Compounds and Their Relationship to Target Organ Injury.
World Life Research Institute. Colton, California © 1995
5 Sacarello, Hildegarde L. The Comprehensive Handbook of Hazardous Materials: Regulations,
Handling, Monitoring, and Safety. Lewis Publishers/CRC Press. Boca Raton, FL © 1994
6 Goldberg, Burton. The Definitive Guide to Alternative Medicine. Future Medicine, Inc., Tiberon, CA © 1995 page 561.
7 IBID. Kyle, Marlene E. and John L. Farber. Pgs 81 & 82.
8 Staninger, Hildegarde. Mycotoxins and Their Effect on the Human Body. World Safety Organization. 17th International Environmental Heath and Safety Conference & Expo 2003 Proceedings. WSO, Warrensburg, MO © 2003
9 Park, Sang-Hwoi. Yamatoshinjo Research. University of Tokyo. Tokyo, Japan. © 2005
10 Staninger, Hildegarde. “What is Far Infrared?” Korean Health Magazine. Los Angeles, CA
Volume 1 © 2004
11 Staninger, Hildegarde. “MSG and Other Glutamates” Korean Health Magazine. Los Angeles, CA. Volume 4 © 2004
12 Potter, Michael. UC San Diego. Image of the Week – Superoxide Dismutase © 2005
www.imageoftheweek.com
13 Infrared Science. www.infraredscience.com © 2005
14 Staninger, Hildegarde. “How Do Genie Spa Spheres Work?” www.geniespaspheres.com
© 2005
15 Staninger, Hildegarde. Superoxide Dismutase 1, 2 and 3. www.pandleylab.com
SOD enzyme genome © 2003 John Hopkins University College of Medicine.
16 www.downsyndromefoundation.com (Oxidative Stress on Down Syndrome Individuals)
17 Hileman, E.A., Achanta, G. and P. Huang. “Superoxide Dismutase: An Emerging Target for Cancer Therapeutics.” Expert Opinion on Therapeutic Targets. 1 December 1002, vol. 5, no. 6 pp. 697-719 (14). Ashley Publications
18 NASA. Biological Crystal Growth in Space – Image of the Week. “Manganese Superoxide Dismutase (MnSOD) Crystal Grown on the International Space Station. Cape Kennedy, Fl © 2005 (www.nasa.com)
19 Kaylor, Mark and Ken Babal. Syndrome X and SX-Fraction. Woodland Publishing. Pleasant Grove, Utah. © 2003
20 Parsons, James Monroe. Hyperbaric Medicine. World Center for Anti-Aging Medicine. Porta Plata, Dominican Republic. © 1995
21 Jung, S., Staninger, H., and D. Farrier. The Definition of True Far Infrared. Research Department. MPS Global, Inc. Pomona, CA © 2004
22 Morgan, Donald P. Recognition and Management of Pesticide Poisonings, 4th Edition. US
EPA, US Government Printing Office, Washington, D.C. © 1989
23 IBID. Handbook of Toxicolgic Pathology. Chapter 19: Cardiovascular and Skeletal Muscular Systems. Academic Press, Inc. New York © 1991
24 Evans, Scott J. and H. Sacarello. Symposium on Short-Term Genetic Bioassays in the Evaluation of Complex Environmental Mixtures. “Genetic Cancer Risk Assessment of Electrophilic Hydrocarbon Mixtures in Subsurface Water Supplies.” Genetic Toxicology Division, Health Effects Research Laboratory, US Environmental Protection Agency, Research Park, North Carolina March 27-29, 1984 (recipient of President Walter Lowrie award Martin Marietta Aerospace, Orlando, FL 1984)
25 Staninger, Hildegarde. “Olive Oil: It’s Medicinal Uses for a Healthier You.” Dragon Environmental Corporation. Sanford, FL © 1998
26 Parker, M.W., Blake. C.C., Barra, D., Bossa, F. , Schinina, M.E., Bannister, W.H. and Bannister, J.V. (1987) Structure identity between the iron and manganese-containing superoxide dismutases. Protein Engineering 1, 393-397.
27 Parker, M.W. and Blake, C.C. (1988) Iron and manganese-containing superoxide dismutases can be distingusished by analysis of their primary structures. FEBS Lett. 229, 377-382.
28 Grace, S.C. (1990) Phylogenic distribution of superoxide dismutase supports an endosymbiotic origin of chloroplasts and mitochondria. Life Sci. 47, 1875-1886.
29 Staninger, Hildegarde. Oaky SmokyTM Analyses Report. US Copyright Office, Washington, D.C. © 2004
30 Staninger, Hildegarde. Kelp and Radiation. Korean Health Magazine. Vol. 5 © 2004
31 Liberman, Shari and ken Babal. Maitake Mushroom and D-fraction. Woodland Publishing.
Orem, Utah. © 2004
32 Staninger, Hildegarde. Bio Clear with Kelp. Why the Earthworm Does Not Get Cancer! Work in progress. © 2005
33 Staninger, Hildegarde. Registeration of Oaky SmokyT nano level superoxide dismutase with Pandey Lab/John Hopkins University College of Medicine and oxybenzone with Small chemical molecules, Harvard University. Research Dept. Capital University of Integrative Medicine, Washington, D.C. and IBHM, Inc., Los Angeles, CA © 2003
34 Beyer, W.F., Jr., Reynolds, J.A., and Fridovich, I. (1980) Differences between the manganese and the iron containing superoxide dismutases of Escherichia coli detected through sedimentation equilibrium, hydrodynamic, and spectroscopic studies. Biochemistry 28, 4403-4409.
35 Sehn, A.P. and Meier, B. (1994) Regulation of an in vivo metalexchangeable superoxide dismutase from Propionibacterium shermanii exhibiting activity with different metal cofactors. Biochem. J. 304, 803-808.
36 Lim, J.H., Yu, Y.G., Han, Y.S., Cho, S. , Ahn, B.Y., Kim, S.H. and Cho. Y. (1997) The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 A resolution: Structural basis for thermostability. J. Mol. Biol. 270, 259-274.
37 Lah, M.S., Dixon, M.M., Pattridge, K.A., Stallings, W.C., Fee, J.A., and Ludwig, M.L. (1995) Structure – function in Escherichia coli iron superoxide dismutase: Comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry 34, 1646-1660.
38 Cooper, J.B., McIntyre, K., Badasso, M.O., Wood, S.P., Garbe, T.R. and Young, D. (1995) Xray structure analysis of the iron dependent superoxide dismutase form Mycobacterium tuberculosis at 2.0 A resolution reveals novel dimer-dimer interactions. J. Mol. Biol. 246, 531-544.
39 Stoddard, B.L., Howell, P.L., Ringe, D. and Petsko, G.A. (1990a) The 2.1 A resolution structure of iron superoxide dismutase from Pseudomonas ovalis. Biochemistry 29, 8885-8893.
40 Schmidt, M. Meier, B., and Parak, F. (1996) Xray structure of the cambialistic superoxide dismutse from Propionibacterium shermanii active with Fe or Mn. J. Biol. Inorg. Chem. 1, 532-541.
41 Borgstahl, G.E.O., M. Pokross, R. Chehab, A. Sekher, and E.H. Snell. (2000) Cryotrapping the sixcoordinate, distored-octahedral active site of manganese superoxide dismutase. J. Mol. Biol. 296:951-959.
42 Loes, Michael. The Healing Power of Jerusalem Artichoke Fiber. Freedom Press, Topanga, CA © 2000.
43 Mjolsness, Alton and H. Staninger. PSP, Inc. largest producer of Jerusalem Artichoke in North America. (Patented seed stock for high FOS yields). Reseach in the nutritional modulation factors of Jerusalem Artichoke powder. Premium Sweetner and Products, Inc., Fargo, North Dakota. 1998 – 2005
44 Wise, John A. Morin, Robert J. , Sanderson, Roger, and Kenneth Blum. Changes in Plasma Carotenoid, Alpha-tocopherol, and Lipid Peroxide Levels in Response to Supplemtnaiton with Concentrated Fruit and Vegetable extracts: A Pilot Study. Current Therapeutic Research. Vol. 57, No. 6, Excerpta Medica, Inc. March 1996
45 Staninger, Hildegarde. The Earthworm: A Microcosmos of “No Disease” as Compared to the Human Being, A Macrocosmos of Chaos and the Disease, Cancer. A Comparative Research Thesis. Capital University of Integrative Medicine. Washington, D.C., Nov. 4, 2001
46 Staninger, Hildegarde. Acoustical Wave Genetics. Page One Science, Inc. Alexandria, VA
© 2005.
(Tables follow in separate thread)
Copyright © 2009 Dr. Hildegarde Staninger, RIET-1
Industrial Toxicologist/IH,
Doctor of Integrative Medicine
Integrative Health Systems, LLC
415 3/4th N. Larchmont Blvd.,
Los Angeles, CA 90004
Tel: 323-466-2599 Fax: 323-466-2774
www.hildegarde-staninger.com
www.healinggrapevine.com
The Future of Superoxid Dismutases and Nutritional Modulation
NASA principal investigator, Dr. Gloria Borgstahl, formerly of the University of Toledo, and now of the University of Nebaraska, has successfully crystallized E. coli manganese superoxide dismutase (MnSOD), antioxidant enzymes that are homologous to those found in cellular mitochondria, on the International Space Station during the period of December 2001 to April 2002. Several of the MnSOD crystals grown on ISS were 80 times greater in crystal volume than earth-grown crystals. Di spots to 1.26 resolutions were observed providing significantly improved data obtained from crystals grown in earth laboratories. An exciting result was that the MnSOD crystals grown on ISS were suitable for neutron studies and time-Laue studies-methods that require large, perfect crystals. With the neutron examples the researchers hope to be able to obtain the, never-before-seen, three-dimensional structure of the hydrogen’s on each amino acid of the protein and thereby be able to answer the unsolved questions concerning the source of these hydrogens in this reaction mechanism. With the time-resolved Laue experiments, the team will be able to generate the superoxide substrate within the crystals with a laser pulse and thus film the “movie” of the enzyme converting it to the products peroxide and water. The enzyme MnSODs in the body is important, and in-depth study of their structure is not to the ability to understand their true function, but these experiments may lead to new therapeutics for the treatment of various degenerative diseases.18
Superoxide dismutases (SODs) are antioxidant metalloenzymes catalyzing the redox disproportion in the (dismutation) of superoxide radical, O2*- as previously discussed in Equation (1).
It is generally accepted that in all SODs the metal ion (M) catalyzes dismutation of the superoxide radical through a cyclic oxidation reduction mechanism:
M3+ + O2*- --> M2+ + O2 (1.1)
M2+ + O2*- + 2H+ ---> M3+ + H2O2 (1.2)
The four classes of SODs are known, distinguished by the metal prosthetic groups: Cu/Zn, FE, Mn and Ni. Fe- and Mn- SODs constitute a structural family.26,27 Fe- and Mn- SODs are unequally distributed throughout the kingdoms of living organisms and are located in different cellular compartments.28,29,30,31 In particular, Fe-SOD is found in obligate anaerobes and aerobic diazotrophs (exclusively), facultative aerobes (exclusively or together with Mn-SOD). In the cytosol of cyanobacteria, in the chloroplast stroma of higher plants, in the protozoa, kelp, Yamatoshinjo and Oaky Smoky (Cu/Zn-SOD, Fe-SOD, Mn-SOD)TM 32,33,34 Fe-SOD and Mn-SOD form some organisms (e.g. Escherichia coli ) exhibit almost absolute metal specificity ,35 while other enzymes, such as “cambialistic” SOD form Propionibacterium shermanii, are captive with either metal.36 Fe- and Mn-SODs occur as homodimers or homotetramiers.
The 3-D structures of several Fe-SODs have been determined. 36,37,38,39,40 The monomers fold into two domains. The N-terminal domain consists of two long antiparallel helices. The C-terminal domain contains a central beta-sheet formed by three antiparallel beta strands with 4-6 surrounding helices. The iron atom is lignaded by two residues from each of the N-terminal helices and two residues from the loops in the C-terminal domain.
The active site iron is pentacoordinate, with the metal lignands (N x epsilon) of three conserved His residues, O x delta of the conserved Asp residue of a water molecule) arranged in distorted trigonal bipyramidal geometry, which opposite of the tetrahydronal molecule of water. The first His residue and a solvent molecule fill the two axial positions. In the azide-FeIII –SOD complex, the iron becomes hexacoodinate with distorted octahedral geometry (similar to the fat soluble Vitamin E), with azide coordinated trans to ASP ligand.41 Table 1 lists the mononuclear iron environment residues in known 3D structures with their PDB Code and Reference.
Superoxide dismutases (SODs) have been found in various nutritional sources such as Jerusalem artichoke powder and Bifidobacterium. 42,43 Juice Plus + Vineyard Blend, foods grown in red clay soils, Yamatoshinjo and hemp oil. 44, 34,45 The use of these nutritional modulators have shown significant risk to oxidative stress via the superoxide radical as they have maintained cellular integrity and reduced cellular sensitization as individual whole foods with an individual’s meals.
Summary
Cells are continuously exposed to a variety of oxidative process which could potentially lead to cellular injury or death. As a result, aerobic organisms possess effective defense mechanisms against oxidative stress as associated with the superoxide radical and improper nutritional modulation that would reduce superoxide dismutases (SODs) in the cell and thereby circumvent toxic cell injury. These protective mechanisms fall into two broad categories: (1) those which prevent the initiation of lipid peroxidation and (2) those which prevent its propagation.
Superoxide dismutase and catalase provide antioxidant protection by inhibiting the formation of the hydroxyl radical. Chelation of the ferric iron necessary for the formation of the hydroxyl radical and direct removal of this species by radical scavengers (e.g., mannital) are also protective. The generation of species capable of initiating peroxidation may exceed the capacity of effectively remove them. Thus, there are other defenses to prevent the uncontrolled propagation of lipid peroxidation and oxidative stress as associated with free oxygen radicals/hydroxyl radicals. These include water-soluble antioxidants, such as ascorbic acid (vitamin C) and reduced glutathione, and fat-soluble antioxidants, most notably alpha-tocopherol (vitamin E). It appears that vitamins E and C and glutathione combine in some as yet poorly defined cycle to donate hydrogen atoms to lipid and/or peroxy radicals, thereby preventing further propagation of the lipid peroxidation, which was initiated by free oxygen radicals.
The metabolism of toxic substances as associated with hazardous materials by mixed function oxidation or other mechanisms leads to irreversible cell injury thorough mechanisms that have been related either to the covalent binding of reactive metabolites, to changes in protein thiols, to alterations in intracellular calcium homeostasis, or to the formation of partially reduced oxygen species. The relative roles that each of these mechanisms plays in any particular example of toxic cell injury remains controversial and a subject of continuing investigation through the advancement of new analytical technologies/equipment. In the case of the various forms of superoxide dismutases, “quickened” advances in science, chemistry and wave genetics 46 will show that these metalloenzymes will play a major character role in the explanation of “creation” through the variable of true far infrared sources, superluminal radiance, the effects of Cooper pairs upon EcceleratedTM intelligent water and the role of the white worm hole found in black holes as recently found in the DNA molecule. These future researchers will be the Indigo and Crystal children – our grand children with their little pet black rabbit with pink ears and a white spot named Ben as it hops down a white worm hole in the quantum biophysics of the human cell. Time and Eternity will show all of us the wonders that will amaze the original Creator of us all through the marvels of science, spirituality, art and medicine.
References
1 U.S. Department of Health, Education, and Welfare. Occupational Diseases: A Guide to Their Recognition. U.S. Government Printing Office, Washington, D.C. Revised Edition June 1977 pgs. 31-41.
2 Kyle, Marlene E. and John L. Farber. Handbook of Toxicologic Pathology. Chapter 6: Biochemical Mechanisms of Toxic Cell Injury. Academic Press, Inc. New York © 1991.
3 Goldberg, Burton. Alternative Medicine Guide to Cancer. Future Medicine, Inc., Tiberon, CA.
pgs, 731-736 Maverick Test by Dr. Hildegarde Staninger. © 1996
4 Staninger, Hildegarde. Maverick Compounds and Their Relationship to Target Organ Injury.
World Life Research Institute. Colton, California © 1995
5 Sacarello, Hildegarde L. The Comprehensive Handbook of Hazardous Materials: Regulations,
Handling, Monitoring, and Safety. Lewis Publishers/CRC Press. Boca Raton, FL © 1994
6 Goldberg, Burton. The Definitive Guide to Alternative Medicine. Future Medicine, Inc., Tiberon, CA © 1995 page 561.
7 IBID. Kyle, Marlene E. and John L. Farber. Pgs 81 & 82.
8 Staninger, Hildegarde. Mycotoxins and Their Effect on the Human Body. World Safety Organization. 17th International Environmental Heath and Safety Conference & Expo 2003 Proceedings. WSO, Warrensburg, MO © 2003
9 Park, Sang-Hwoi. Yamatoshinjo Research. University of Tokyo. Tokyo, Japan. © 2005
10 Staninger, Hildegarde. “What is Far Infrared?” Korean Health Magazine. Los Angeles, CA
Volume 1 © 2004
11 Staninger, Hildegarde. “MSG and Other Glutamates” Korean Health Magazine. Los Angeles, CA. Volume 4 © 2004
12 Potter, Michael. UC San Diego. Image of the Week – Superoxide Dismutase © 2005
www.imageoftheweek.com
13 Infrared Science. www.infraredscience.com © 2005
14 Staninger, Hildegarde. “How Do Genie Spa Spheres Work?” www.geniespaspheres.com
© 2005
15 Staninger, Hildegarde. Superoxide Dismutase 1, 2 and 3. www.pandleylab.com
SOD enzyme genome © 2003 John Hopkins University College of Medicine.
16 www.downsyndromefoundation.com (Oxidative Stress on Down Syndrome Individuals)
17 Hileman, E.A., Achanta, G. and P. Huang. “Superoxide Dismutase: An Emerging Target for Cancer Therapeutics.” Expert Opinion on Therapeutic Targets. 1 December 1002, vol. 5, no. 6 pp. 697-719 (14). Ashley Publications
18 NASA. Biological Crystal Growth in Space – Image of the Week. “Manganese Superoxide Dismutase (MnSOD) Crystal Grown on the International Space Station. Cape Kennedy, Fl © 2005 (www.nasa.com)
19 Kaylor, Mark and Ken Babal. Syndrome X and SX-Fraction. Woodland Publishing. Pleasant Grove, Utah. © 2003
20 Parsons, James Monroe. Hyperbaric Medicine. World Center for Anti-Aging Medicine. Porta Plata, Dominican Republic. © 1995
21 Jung, S., Staninger, H., and D. Farrier. The Definition of True Far Infrared. Research Department. MPS Global, Inc. Pomona, CA © 2004
22 Morgan, Donald P. Recognition and Management of Pesticide Poisonings, 4th Edition. US
EPA, US Government Printing Office, Washington, D.C. © 1989
23 IBID. Handbook of Toxicolgic Pathology. Chapter 19: Cardiovascular and Skeletal Muscular Systems. Academic Press, Inc. New York © 1991
24 Evans, Scott J. and H. Sacarello. Symposium on Short-Term Genetic Bioassays in the Evaluation of Complex Environmental Mixtures. “Genetic Cancer Risk Assessment of Electrophilic Hydrocarbon Mixtures in Subsurface Water Supplies.” Genetic Toxicology Division, Health Effects Research Laboratory, US Environmental Protection Agency, Research Park, North Carolina March 27-29, 1984 (recipient of President Walter Lowrie award Martin Marietta Aerospace, Orlando, FL 1984)
25 Staninger, Hildegarde. “Olive Oil: It’s Medicinal Uses for a Healthier You.” Dragon Environmental Corporation. Sanford, FL © 1998
26 Parker, M.W., Blake. C.C., Barra, D., Bossa, F. , Schinina, M.E., Bannister, W.H. and Bannister, J.V. (1987) Structure identity between the iron and manganese-containing superoxide dismutases. Protein Engineering 1, 393-397.
27 Parker, M.W. and Blake, C.C. (1988) Iron and manganese-containing superoxide dismutases can be distingusished by analysis of their primary structures. FEBS Lett. 229, 377-382.
28 Grace, S.C. (1990) Phylogenic distribution of superoxide dismutase supports an endosymbiotic origin of chloroplasts and mitochondria. Life Sci. 47, 1875-1886.
29 Staninger, Hildegarde. Oaky SmokyTM Analyses Report. US Copyright Office, Washington, D.C. © 2004
30 Staninger, Hildegarde. Kelp and Radiation. Korean Health Magazine. Vol. 5 © 2004
31 Liberman, Shari and ken Babal. Maitake Mushroom and D-fraction. Woodland Publishing.
Orem, Utah. © 2004
32 Staninger, Hildegarde. Bio Clear with Kelp. Why the Earthworm Does Not Get Cancer! Work in progress. © 2005
33 Staninger, Hildegarde. Registeration of Oaky SmokyT nano level superoxide dismutase with Pandey Lab/John Hopkins University College of Medicine and oxybenzone with Small chemical molecules, Harvard University. Research Dept. Capital University of Integrative Medicine, Washington, D.C. and IBHM, Inc., Los Angeles, CA © 2003
34 Beyer, W.F., Jr., Reynolds, J.A., and Fridovich, I. (1980) Differences between the manganese and the iron containing superoxide dismutases of Escherichia coli detected through sedimentation equilibrium, hydrodynamic, and spectroscopic studies. Biochemistry 28, 4403-4409.
35 Sehn, A.P. and Meier, B. (1994) Regulation of an in vivo metalexchangeable superoxide dismutase from Propionibacterium shermanii exhibiting activity with different metal cofactors. Biochem. J. 304, 803-808.
36 Lim, J.H., Yu, Y.G., Han, Y.S., Cho, S. , Ahn, B.Y., Kim, S.H. and Cho. Y. (1997) The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 A resolution: Structural basis for thermostability. J. Mol. Biol. 270, 259-274.
37 Lah, M.S., Dixon, M.M., Pattridge, K.A., Stallings, W.C., Fee, J.A., and Ludwig, M.L. (1995) Structure – function in Escherichia coli iron superoxide dismutase: Comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry 34, 1646-1660.
38 Cooper, J.B., McIntyre, K., Badasso, M.O., Wood, S.P., Garbe, T.R. and Young, D. (1995) Xray structure analysis of the iron dependent superoxide dismutase form Mycobacterium tuberculosis at 2.0 A resolution reveals novel dimer-dimer interactions. J. Mol. Biol. 246, 531-544.
39 Stoddard, B.L., Howell, P.L., Ringe, D. and Petsko, G.A. (1990a) The 2.1 A resolution structure of iron superoxide dismutase from Pseudomonas ovalis. Biochemistry 29, 8885-8893.
40 Schmidt, M. Meier, B., and Parak, F. (1996) Xray structure of the cambialistic superoxide dismutse from Propionibacterium shermanii active with Fe or Mn. J. Biol. Inorg. Chem. 1, 532-541.
41 Borgstahl, G.E.O., M. Pokross, R. Chehab, A. Sekher, and E.H. Snell. (2000) Cryotrapping the sixcoordinate, distored-octahedral active site of manganese superoxide dismutase. J. Mol. Biol. 296:951-959.
42 Loes, Michael. The Healing Power of Jerusalem Artichoke Fiber. Freedom Press, Topanga, CA © 2000.
43 Mjolsness, Alton and H. Staninger. PSP, Inc. largest producer of Jerusalem Artichoke in North America. (Patented seed stock for high FOS yields). Reseach in the nutritional modulation factors of Jerusalem Artichoke powder. Premium Sweetner and Products, Inc., Fargo, North Dakota. 1998 – 2005
44 Wise, John A. Morin, Robert J. , Sanderson, Roger, and Kenneth Blum. Changes in Plasma Carotenoid, Alpha-tocopherol, and Lipid Peroxide Levels in Response to Supplemtnaiton with Concentrated Fruit and Vegetable extracts: A Pilot Study. Current Therapeutic Research. Vol. 57, No. 6, Excerpta Medica, Inc. March 1996
45 Staninger, Hildegarde. The Earthworm: A Microcosmos of “No Disease” as Compared to the Human Being, A Macrocosmos of Chaos and the Disease, Cancer. A Comparative Research Thesis. Capital University of Integrative Medicine. Washington, D.C., Nov. 4, 2001
46 Staninger, Hildegarde. Acoustical Wave Genetics. Page One Science, Inc. Alexandria, VA
© 2005.
(Tables follow in separate thread)