The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.
Open accessAbstract
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Transport is facilitated by multicopper ferroxidases including the abundant serum protein ceruloplasmin and its membrane-bound intestinal homolog hephaestin.”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [81]
Citations
Cites
Mack, H. C. (1960) · Clinical Obstetrics & Gynecology · doi:10.1097/00003081-196006000-00007 · Cited by 929
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
Koechlin, B. A. (1952) · Journal of the American Chemical Society · doi:10.1021/ja01130a054 · Cited by 124
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
Determination of Ceruloplasmin Oxidase in Serum
Henry, R. J. W., Chiamori, N., Jacobs, S., & SEGALOVE, M. (1960) · Experimental Biology and Medicine · doi:10.3181/00379727-104-25928 · Cited by 81
Report of the Commission on Enzymes of the International Union of Biochemistry, 1961
(1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60268-6 · Cited by 79
A coupled iron-caeruloplasmin oxidation system
Curzon, G., & O’Reilly, S. (1960) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(60)90185-6 · Cited by 78
Proof for the Ascorbate Oxidase Activity of Ceruloplasmin
Osaki, S., McDermott, J. A., & Frieden, E. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97760-4 · Cited by 64
Self-citationSome properties of coupled iron–caeruloplasmin oxidation systems
Curzon, G. (1961) · Biochemical Journal · doi:10.1042/bj0790656 · Cited by 64
Chase, M., Gubler, C. J., Cartwright, G. E., & Wintrobe, M. M. (1952) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38514-4 · Cited by 51
Is Ceruloplasmin an Ascorbic Acid Oxidase?
Morell, A. G., Aisen, P., & Scheinberg, I. H. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70838-2 · Cited by 42
Walshe, J. M. (1963) · Journal of Clinical Investigation · doi:10.1172/jci104790 · Cited by 16
Über eine im intermediären Eisenstoffwechsel entstehende Ferriglobulinverbindung
Starkenstein, E., & Harvalik, Z. (1933) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/bf01860483 · Cited by 16
Die Bedingungen der Oxydation des Eisens im Blute
Hendrych, F., & Mori, S. (1933) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/bf01860476 · Cited by 4
Research works printed but not linked: 3
- 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
Cited by
Sorted by citations
[1] Role of free radicals and catalytic metal ions in human disease: An overview
Halliwell, B., & Gutteridge, J. M. C. (1990) · Methods in Enzymology · doi:10.1016/0076-6879(90)86093-b · Cited by 4,994
Multicopper oxidases and oxygenases
Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996) · Chemical Reviews · doi:10.1021/cr950046o · Cited by 3,664
Copper Active Sites in Biology
Solomon, E. I., Heppner, D. E., Johnston, E. M., Ginsbach, J. W., Cirera, J., Qayyum, M. F., Kieber‐Emmons, M. T., Kjaergaard, C. H., Hadt, R. G., & Tian, L. (2014) · Chemical Reviews · doi:10.1021/cr400327t · Cited by 1,795
Ala, A., Walker, A. P., Ashkan, K., Dooley, J. S., & Schilsky, M. L. (2007) · The Lancet · doi:10.1016/s0140-6736(07)60196-2 · Cited by 1,449
Role of metals in oxygen radical reactions
Aust, S. D., Morehouse, L. A., & Thomas, C. E. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90025-x · Cited by 1,150
Metadata
- 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)
- 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
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review