Document Detail


The purification and characterization of bovine C4, the fourth component of complement.
MedLine Citation:
PMID:  312644     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The fourth component of complement, C4, was isolated from bovine plasma in high yield, by using simple purification techniques. The protein, like human component C4, is a beta-globulin with a mol.wt. of about 200 000 and consists of three polypeptide chains, alpha, beta and gamma, with apparent mol. wts. of 98 000, 82 000 and 32 000 respectively. The chains of C4 have been separated by methods previously used for human C4. Their amino acid compositions are very similar to those of the human component, but differences in carbohydrate distribution have been observed. The haemolytic activity of bovine C4 is totally destroyed by incubation with bovine C1s, the activated subcomponent of the first component of complement. Component C4, treated in this way, was shown to be cleaved in the alpha chain, which was decreased in mol.wt. by about 9000, corresponding to the removal of subcomponent C4a.
Authors:
N A Booth; R D Campbell; J E Fothergill
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  177     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1979 Mar 
Date Detail:
Created Date:  1979-07-25     Completed Date:  1979-07-25     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  959-65     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Animals
Carbohydrates / analysis
Cattle
Complement C1s
Complement C4 / immunology,  isolation & purification*
Hemolysis
Molecular Weight
Peptides / isolation & purification
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Carbohydrates; 0/Complement C4; 0/Peptides; EC 3.4.21.42/Complement C1s
Comments/Corrections

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