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PMID: 6215918 Published · ppublish English Journal Article

Purification and structural studies on the complement-system control protein beta 1H (Factor H).

The Biochemical journal ·Vol. 205 ·No. 2 ·1982-08-01 ·Pages 285-93

Sim RB, DiScipio RG

Abstract

An efficient procedure for the isolation of the complement-system control protein beta 1H (Factor H) from human plasma was developed. The chemical composition and physical characteristics of the protein were studied, and a sequence of 17 amino acid residues at the N-terminus was determined. Factor H is a single-polypeptide-chain glycoprotein of mol.wt. 155 000 containing 9.3% carbohydrate. Factor H is cleaved by plasma proteinases to a two-chain form. This cleavage can be mimicked by trypsin, and the two-chain form retains fully the C3b-inactivator cofactor activity of Factor H. The proteolytic fragments of Factor H are compared with those of other proteins (C4b-binding protein and erythrocyte C3b-receptor) that act as cofactors for C3b-inactivator.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Carbohydrates/analysis Chromatography, Gel Chromatography, Ion Exchange Complement C3b Inactivator Proteins/isolation & purification Complement Factor H Electrophoresis, Polyacrylamide Gel Humans Molecular Weight Peptide Fragments/analysis
Chemicals
Amino Acids CFH protein, human Carbohydrates Complement C3b Inactivator Proteins Peptide Fragments Complement Factor H
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sim R B
DiScipio R G
References (36)
36 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1982-08-01
Pages
285-93
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1158480
Subset
IM
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