Crossref journal-article
Portland Press Ltd.
Biochemical Journal (288)
Abstract

The manner in which human liver cathepsin B (EC 3.4.22.1) digests glucagon was determined. After reaction of the proteinase with the substrate for 24h, more than 15 products were formed. During the first 7 h of reaction, eight products were formed; seven of these were dipeptides that originated from the C-terminal portion of the glucagon molecule, whereas the eighth peptide was the remaining large fragment of the hormone, consisting of residues 1-19. Measurement of the rate of formation of the products showed that cathepsin B degraded glucagon by a sequential cleavage of dipeptides from the C-terminal end of the molecule. Cathepsin B from both rat liver and bovine spleen was shown to hydrolyse glucagon by the same mechanism.

Bibliography

Aronson, N. N., & Barrett, A. J. (1978). The specificity of cathepsin B. Hydrolysis of glucagon at the C-terminus by a peptidyldipeptidase mechanism. Biochemical Journal, 171(3), 759–765.

Authors 2
  1. N N Aronson (first)
  2. A J Barrett (additional)
References 0 Referenced 127

None

Dates
Type When
Created 10 years ago (Aug. 10, 2015, 4:10 p.m.)
Deposited 3 years, 9 months ago (Nov. 26, 2021, 12:50 p.m.)
Indexed 1 month, 3 weeks ago (July 2, 2025, 3:10 p.m.)
Issued 47 years, 2 months ago (June 1, 1978)
Published 47 years, 2 months ago (June 1, 1978)
Published Print 47 years, 2 months ago (June 1, 1978)
Funders 0

None

@article{Aronson_1978, title={The specificity of cathepsin B. Hydrolysis of glucagon at the C-terminus by a peptidyldipeptidase mechanism}, volume={171}, ISSN={0264-6021}, url={http://dx.doi.org/10.1042/bj1710759}, DOI={10.1042/bj1710759}, number={3}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Aronson, N N and Barrett, A J}, year={1978}, month=jun, pages={759–765} }