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

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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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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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