Cited by 679Iron Metabolism and DisordersMetal-Catalyzed Oxygenation MechanismsTrace Elements in Health

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The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.

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Osaki, Shigemasa, Johnson, Donald A., Frieden, Earl·1966·Journal of Biological Chemistry

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Abstract

The oxidation of Fe(II) by serum was studied at pH 7.35 and at various oxygen concentrations which approach the physiological conditions of human serum. The nonenzymic oxidation of Fe(II) was estimated to be insufficient to account for a rate of Fe(III)-transferrin formation necessary to provide an adequate iron supply for hemoglobin and other biosyntheses if Fe(II) is a relevant source of serum iron. The results suggested that an appreciable catalytic activity was involved in Fe(II) oxidation in serum. The ferroxidase activity of various normal human sera correlates precisely with the p-phenylenediamine oxidase activity of these sera. This catalytic activity is inhibited by azide and cyanide, and is low in sera with reduced ceruloplasmin levels. Fe(II) oxidation is also associated with the ceruloplasmin fraction on diethylaminoethyl cellulose chromatography of serum. The oxidation of Fe(II) by ceruloplasmin is zero order with respect to oxygen (10 to 200 µm), whereas the nonenzymic oxidation is first order. A biological role for the ceruloplasmin of serum in promoting the rate of iron saturation of transferrin and in stimulating iron utilization and the designation of the enzyme as serum ferroxidase is proposed.

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THE PLASMA PROTEINS
Mack, H. C. (1960) · Clinical Obstetrics & Gynecology · doi:10.1097/00003081-196006000-00007 · Cited by 929
Investigations in Serum Copper. II. Isolation of the Copper Containing Protein, and a Description of some of its Properties.
Holmberg, C. G., Laurell, C. ‐., & Gjertsen, P. (1948) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.02-0550 · Cited by 472
THE PLASMA-TO-CELL CYCLE OF TRANSFERRIN*
Jandl, J. H., & Katz, J. H. (1963) · Journal of Clinical Investigation · doi:10.1172/jci104718 · Cited by 440
The specific binding of iron(III) and copper(II) to transferrin and conalbumin
Aasa, R., Malmström, B. G., Saltman, P., & Vänngård, T. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)90599-7 · Cited by 366
TRANSFER OF IRON FROM SERUM IRON-BINDING PROTEIN TO HUMAN RETICULOCYTES*
Jandl, J. H., Inman, J. K., Simmons, R. L., & Allen, D. W. (1959) · Journal of Clinical Investigation · doi:10.1172/jci103786 · Cited by 353
THE QUANTITATIVE DETERMINATION OF IRON KINETICS AND HEMOGLOBIN SYNTHESIS IN HUMAN SUBJECTS*
Pollycove, M., & Mortimer, R. G. (1961) · Journal of Clinical Investigation · doi:10.1172/jci104310 · Cited by 231
Preparation and Properties of Serum and Plasma Proteins. XXVIII. The β1-Metal-combining Protein of Human Plasma1a, b
Koechlin, B. A. (1952) · Journal of the American Chemical Society · doi:10.1021/ja01130a054 · Cited by 124
STUDIES IN IRON TRANSPORTATION AND METABOLISM. IV. OBSERVATIONS ON THE ABSORPTION OF IRON FROM THE GASTRO-INTESTINAL TRACT 12
Moore, C. V., Arrowsmith, W. R., Welch, J., & Minnich, V. (1939) · Journal of Clinical Investigation · doi:10.1172/jci101069 · Cited by 105
The role of chelation in iron metabolism
Saltman, P. (1965) · Journal of Chemical Education · doi:10.1021/ed042p682 · Cited by 101
Studies on the Exchange of Iron between Transferrin and Reticulocytes
Morgan, E. H., & Laurell, C. ‐. (1963) · British Journal of Haematology · doi:10.1111/j.1365-2141.1963.tb05471.x · Cited by 88

Show all 20 references

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Osaki, S., McDermott, J. A., Johnson, D. A., and Frieden, E., in J. Peisach, W. Blumberg, and P. Aisen (Editors), International Symposium on the Biochemistry of Copper, Academic Press, Inc., New York, in press.
Trader, 1965, Federation Proc., 24, 222
Broman, 1964, Acta Soc. Med. Upsalien., 69, 75

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Sabatucci, A., Vachette, P., Vasilyev, V. B., Beltramini, M., Av, S., Pulina, M. O., Salvato, B., Angelucci, C. B., Maccarrone, M., Cozzani, I., et al. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.089 · Cited by 36
Physiology and pharmacology of copper
Österberg, R. (1980) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(80)90019-4 · Cited by 36
The incorporation of iron into apoferritin as mediated by ceruloplasmin
Boyer, R. F., & Schori, B. E. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(83)90407-2 · Cited by 36
Purification and properties of bovine caeruloplasmin
Calabrese, L., Malatesta, F., & Barra, D. (1981) · Biochemical Journal · doi:10.1042/bj1990667 · Cited by 36
Acute phase responses to experimental salmonellosis in calves and colibacillosis in chickens: Serum iron and caeruloplasmin
Piercy, D. W. T. (1979) · Journal of Comparative Pathology · doi:10.1016/0021-9975(79)90020-3 · Cited by 35
Thiol‐linked peroxidase activity of human ceruloplasmin
Kim, I. G., Park, S. Y., Kim, K. C., & Yum, J. J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00817-5 · Cited by 35
Disruption of iron homeostasis and resultant health effects upon exposure to various environmental pollutants: A critical review
Guo, W., Zhang, J., Li, W., Xu, M., & Liu, S. (2015) · Journal of Environmental Sciences · doi:10.1016/j.jes.2015.04.004 · Cited by 35
Ceruloplasmin: Methods and Clinical Use
Wolf, P. L., & Griffiths, J. G. (1982) · CRC Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408368209107037 · Cited by 34
Copper in human and animal health
Harris, E. D. (1983) · Elsevier eBooks · doi:10.1016/b978-0-407-00255-5.50009-4 · Cited by 34
ASCORBATE OXIDASE AND RELATED COPPER PROTEINS
Dawson, C. R., Strothkamp, K. G., & Krul, K. G. (1975) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1975.tb29281.x · Cited by 34
Case of presymptomatic aceruloplasminemia treated with deferasirox
Tai, M., Matsuhashi, N., Ichii, O., Suzuki, T., Ejiri, Y., Kono, S., Terada, T., Miyajima, H., & Harada, M. (2013) · Hepatology Research · doi:10.1111/hepr.12292 · Cited by 33
Clinical Implications of New Insights into Hepcidin-Mediated Regulation of Iron Absorption and Metabolism
Prentice, A. M. (2017) · Annals of Nutrition and Metabolism · doi:10.1159/000480743 · Cited by 38
Ceruloplasmin Upregulation in Retina of Murine and Human Glaucomatous Eyes
Stasi, K., Nagel, D., Yang, X., Ren, L., Mittag, T. W., & Danias, J. (2007) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.06-0497 · Cited by 33
Effect of pH on Electron‐Paramagnetic‐Resonance Spectra of Ceruloplasmin
Gunnarsson, P., Nylén, U., & Pettersson, G. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb02955.x · Cited by 33
The structure of BAcillus subtilis levansucrase at 3.8 A resolution.
Lebrun, É., & Rapenbusch, R. V. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70239-7 · Cited by 33
Ironing Out the Unconventional Mechanisms of Iron Acquisition and Gene Regulation in Chlamydia
Pokorzynski, N. D., Thompson, C. C., & Carabeo, R. A. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00394 · Cited by 33
Studies of the ceruloplasmin-lactoferrin complex
Pulina, M. O., Zakharova, E. T., Av, S., Shavlovski, M. M., Bass, M. G., Solovyov, K. V., Kokryakov, V. N., & Vasilyev, V. B. (2002) · Biochemistry and Cell Biology · doi:10.1139/o01-206 · Cited by 32
Selected Features of Copper Metabolism in the Cat
Doong, G., Keen, C. L., Rogers, Q. R., Morris, J., & Rucker, R. B. (1983) · Journal of Nutrition · doi:10.1093/jn/113.10.1963 · Cited by 32
Influence of Sucrose and Starch on the Development of Anemia in Copper- and Iron-Deficient Rats
Johnson, M. A., & Gratzek, J. M. (1986) · Journal of Nutrition · doi:10.1093/jn/116.12.2443 · Cited by 32
Copper in Mammalian Reproduction
Oster, G., & Salgo, M. (1977) · Advances in pharmacology · doi:10.1016/s1054-3589(08)60191-x · Cited by 32
Rat ceruloplasmin: Resistance to proteolysis and kinetic comparison with human ceruloplasmin
Ryan, T. P., Grover, T. A., & Aust, S. D. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90357-3 · Cited by 32

Authors: Osaki, S., Johnson, D. A., & Frieden, E.
Affiliations: Florida State University (US)
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1966-06
Volume: 241
Issue: 12
Pages: 2746-2751
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)96527-0
OpenAlex: W1508143080
Cited by: 679
References: 20
Citations by year: 2026: 2 · 2025: 5 · 2024: 8 · 2023: 10 · 2022: 10 · 2021: 18 · 2020: 7 · 2019: 12 · 2018: 15 · 2017: 9 · 2016: 15 · 2015: 17 · 2014: 21 · 2013: 16 · 2012: 17
FWCI: 8.81
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 19868 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Keywords: ceruloplasmin, ferroxidase activity, iron(II) oxidation, serum iron, oxygen dependence, iron metabolism
MeSH terms: Aniline Compounds, Humans, Iron, Oxidoreductases, Spectrophotometry, Transferrin, In Vitro Techniques

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The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.

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