Use of dipeptidyl aminopeptidase I (Chathepsin C) for sequence analysis of peptides. | [Journal of Chemical Society of Pakistan • 1987]

Author(s):

1. Ikram Ullah Khan: Gomal University, Dera Ismail Khan, Pakistan

2. Ahmad Saeed: Gomal University, Dera Ismail Khan, Pakistan

3. Masood R. Baig: Gomal University, Dera Ismail Khan, Pakistan

Abstract:

Possible method for the determination of amino acid sequence of polypeptides involves their degradation into dipeptide fragements with dipeptidyl amino peptidase I (Cathepsin C). The action of the enzyme was characterized on different model peptides of known structure. Some tryptic peptides of rabbit muscle aldolase were isolated by gel filtration on Sephadex G-25 column and purified by electrophoretic and chromatographic methods. These peptides and synthetic peptide ACTH1-32 were subjected to dipeptidyl aminopeptidase I digestion. The yield of the dipeptides were reasonable good and the structure of the dipeptides was determined by dansyl-Edman method, thin layer ion exchange chromatography and high voltage electrophoresis. The action of dipeptidyl aminopeptidase I (Catheps in C) was completely inhibited by internal prolyl residues

Page(s): 79-86

DOI: DOI not available

Published: Journal: Journal of Chemical Society of Pakistan, Volume: 9, Issue: 1, Year: 1987

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