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. 1968 Aug;109(1):107–120. doi: 10.1042/bj1090107

Preparation and analysis of peptide fragments produced by pepsin hydrolysis of human plasma albumin and their relationship to its structure

G Franglen 1, G R E Swaniker 1,*
PMCID: PMC1186759  PMID: 4876098

Abstract

Human plasma albumin was prepared and subjected to proteolysis by pepsin at pH2·45 at 25° for 10min. with albumin/pepsin ratio 3000:1. Five peptide fragments were detected in the proteolysate by means of zone electrophoresis and gel filtration; these were separated and purified. Molecular weights, amino acid composition and disulphide bond content of the purified fragments were determined. The results show that a high proportion of the polypeptide chain of albumin appears to have a low cystine content, and at low pH values the molecule would be expected to have a considerable degree of freedom in its structure in these regions of the chain. A tripartite model for the structure of plasma albumin is proposed.

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Selected References

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