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The effects of lactoyl-pepstatin and the pepsin inhibitor peptide on pig cathepsin D.

Year: 1982

Type: article

Abstract: Lactoyl-pepstatin (an acylated tetrapeptide) is much more readily soluble in aqueous media than the more common isovaleryl- and acetyl-pepstatins (acylated pentapeptides). However, the K1 value for inhibition of cathepsin D by lactoyl-pepstatin at pH 3.5 is approx. 10(-7) M, some two to three orders of magnitude weaker than has been obtained previously for isovaleryl- or acetyl-pepstatins. One of the peptides released during activation of pig pepsinogen is known to be an effective inhibitor of pig pepsin, but it does not alter the activity of the similar aspartic proteinase, pig cathepsin D.

Source: Biochemical Journal

DOI: 10.1042/bj2030795

Authors: J Kay, E G Afting, T Aoyagi, B M Dunn

Institutions: University of Florida, University of Göttingen, Cardiff University, University of Wales

Language: English

Topic: Protease and Inhibitor Mechanisms

Subfield: Cancer Research

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: Wellcome Trust, Deutsche Forschungsgemeinschaft, National Institutes of Health

OpenAlex ID: W1866017395

FWCI: 0.859

Cites: 17

Cited by: 8

Related to: 10