Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A rapid and simole procedure for isolation of ceruloplasmin from porcine and bovine blood sera was elaborated; it involves DEAE-Sephadex A-50 chromatography, precipitation with an ethanol-chloroform mixture plus extraction with saline, and preparative polyacrylamide-gel electrophoresis. The preparations obtained showed a high degree of electrophoretic homogeneity and a higher A610/A280 ratio and specific activity than the preparations obtained by the modified method of Broman & Kjellin (Biochem. Biophys. Acta, 82, 101-109, 1964).
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PMID:A simple and rapid procedure for isolation of ceruloplasmin from porcine and bovine blood serum. 75 62

The preparation and properties of ceruloplasmin from goose blood plasma are described. Ammonium sulfate was used to precipitate the crude protein followed by adsorption and elution from DEAE-Sephadex A-50. Further treatment with an ethanol-chloroform mixture and Sephadex G-200 yielded an intensely blue protein possessing a high degree of chemical purity and biological activity. Goose ceruloplasmin, existing in two forms, appears to be a single polypeptide, apparent Mr121,300, with an A610/A280 ratio of 0.07. Copper represented 0.32%, which corresponded to six atoms of copper per protein molecule. Although the amount of EPR-detectable copper was the same as in mammalian ceruloplasmins there were some differences in EPR parameters, mainly in A parallel. Goose ceruloplasmin's amino acid composition, although similar in many residues to human ceruloplasmin, was lower in tyrosine, cystine/cysteine, and acidic amino acids. Valine was found as the N-terminal amino acid. Hexose, hexosamine, sialic acid, and fucose accounted for 6.65% of the weight. Goose protein contained only half the sialic acid of human ceruloplasmin. Two values for Km using either p-phenylenediamine (0.64 and 0.053 mM) or o-dianisidine (0.76 and 0.15 mM) were evaluated from Lineweaver-Burk plots. EPR studies on reactions with water radiolysis products at cryogenic temperatures allowed us to discover that goose ceruloplasmin, like human and bovine ceruloplasmins, possesses superoxide dismutase activity.
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PMID:Purification and partial characterization of goose ceruloplasmin. 282 26

The preparation and properties of ceruloplasmin from chicken serum are described. Ethanol-CHCl3 was used to precipitate the crude protein, followed by adsorption and elution from DEAE-Sephadex. Further treatment with Sephadex G-200 and CM-Sephadex yielded an intensely blue protein judged 1572-fold purer than starting serum. epsilon-Aminocaproic acid (0.02 M) was present in all buffers and starting sera. Chicken ceruloplasmin appears to be a single polypeptide, apparent Mr 124,000, with an A610/A280 ratio of 0.07 and an absorption maximum at 602 nm. Hexose, hexosamine, and sialic acid accounted for 7.2% of the weight; copper represented 0.20%, which suggested four or five copper atoms per molecule. Chicken ceruloplasmin catalyzed the azide-sensitive oxidation of p-phenylenediamine (PPD) and N,N'-dimethyl-p-phenylenediamine (DPD), and showed ferroxidase activity similar to that of human ceruloplasmin. Its amino acid composition, although similar in many residues to human ceruloplasmin, was decidedly lower in methionine and tyrosine. The chicken protein had one-third the sialic acid content of human ceruloplasmin and showed immunochemical nonidentity with human ceruloplasmin.
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PMID:Purification and partial characterization of ceruloplasmin from chicken serum. 403 97

Ceruloplasmin, a copper carrier protein in mammal serum, was isolated by a variation of the Neo-Zgirski method consisting of a chromatography column in DEAE Sephadex A-50 gel, using different buffers for its selective elution. This protein was then precipitated with ammonium sulfate and an ethanol chloroform mixture. Finally, a dialysis against sodium acetate was performed and the samples were purified. In addition, the protein concentration and its characterization were determined. Enzyme kinetics were calculated using paraphenylenediamine as an artificial substrate, determined by the Michaelis constant. Furthermore, an SDS electrophoresis in polyacrylamide gel was performed, and the samples of porcine ceruloplasmin were compared with commercial bovine ceruloplasmin. Finally, a comparative study was carried out between the ceruloplasmin levels in serum from patients with chronic renal insufficiency (CRI) undergoing hemodialysis treatment in artificial kidneys with a cuprophan membrane, with a control group of donors. A similar study was performed with a group of patients suffering from the same illness, but undergoing dialysis treatment with polyacrylonitrile membrane. These results were expressed in mg% in relation to the ceruloplasmin isolated previously.
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PMID:Study of ceruloplasmin in renal insufficiency. 833 18