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. 1981 Sep 1;197(3):573–580. doi: 10.1042/bj1970573

Subunit structured of pig small-intestinal brush-border aminopeptidase N.

A Benajiba, S Maroux
PMCID: PMC1163168  PMID: 6119979

Abstract

Aminopeptidase N (EC 3.4.11.2), when isolated from pig intestine in either the proteinase- or detergent-released form, frequently appears to contain three polypeptide chains, here termed alpha, beta and gamma. We have established by an immunological technique that the beta- and gamma-polypeptides are derived from the alpha-chain and that the intact enzyme is a dimer, alpha 2. Each alpha-chain of the detergent form was shown to contain a hydrophobic anchor peptide about 35 amino acid residues in length, which included the N-terminal sequences. A peptide bond in the alpha-chain was very sensitive to proteolysis. Its cleavage generated the commonly observed forms: alpha beta gamma and beta 2 gamma 2. The gamma-fragment, which lacked the anchor peptide, was derived from the C-terminal part of the alpha-chain.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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