| Literature DB >> 4860638 |
Abstract
Methods are described for the isolation and purification of pepsin D, an enzyme which accounts for about 10% of the enzymic activity in commercial preparations of pepsin. Pepsin D is similar to pepsin in having a molecular weight of about 35000, the same C-terminal amino acid sequence, and an N-terminal isoleucine residue. It differs in having no phosphate residue. Pepsin D is similar to pepsin in its ability to digest haemoglobin, acetyl-l-phenylalanyl-l-di-iodotyrosine and gelatin but it is twice as active as pepsin in the clotting of milk. It has the same specificity as pepsin in its action on the B-chain of oxidized insulin. It is probable that the pepsin D in commercial preparations of pepsin arises from the activation of gastric pepsinogen D.Entities:
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Year: 1967 PMID: 4860638 PMCID: PMC1271214 DOI: 10.1042/bj1040742
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857