Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases.
Salvesen, Guy ; Parkes, Catherine ; Abrahamson, Magnus LU ; Grubb, Anders LU
and Barrett, Alan J
(1986)
In Biochemical Journal
234(2).
p.429-434
- Abstract
- We point out that human low-Mr kininogen contains three cystatin-like sequences, rather than two, as had previously been thought. The protein was purified by affinity chromatography on carboxymethyl-papain-Sepharose, and subjected to limited proteolysis by trypsin and chymotrypsin. Fragments were isolated, and three corresponding to the individual cystatin-like domains were identified. By comparison with the known amino acid sequence of the protein they were numbered 1 to 3 from the N-terminus. Domain 1 was not found to have any inhibitory activity for cysteine proteinases, which is consistent with the absence of residues that are highly conserved in inhibitors of the cystatin superfamily, and have previously been suggested to be essential... (More)
- We point out that human low-Mr kininogen contains three cystatin-like sequences, rather than two, as had previously been thought. The protein was purified by affinity chromatography on carboxymethyl-papain-Sepharose, and subjected to limited proteolysis by trypsin and chymotrypsin. Fragments were isolated, and three corresponding to the individual cystatin-like domains were identified. By comparison with the known amino acid sequence of the protein they were numbered 1 to 3 from the N-terminus. Domain 1 was not found to have any inhibitory activity for cysteine proteinases, which is consistent with the absence of residues that are highly conserved in inhibitors of the cystatin superfamily, and have previously been suggested to be essential for activity. Domain 2 was a good inhibitor of chicken calpain, and also papain and cathepsin L. Domain 3 showed negligible inhibition of calpain, but inhibited papain and cathepsin L strongly. The probable arrangement of disulphide bonds in the heavy chain of low-Mr kininogen is deduced from the homology with the cystatins and other evidence contained in the present paper. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1103691
- author
- Salvesen, Guy
; Parkes, Catherine
; Abrahamson, Magnus
LU
; Grubb, Anders
LU
and Barrett, Alan J
- organization
- publishing date
- 1986
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemical Journal
- volume
- 234
- issue
- 2
- pages
- 429 - 434
- publisher
- Portland Press
- external identifiers
-
- scopus:0022555509
- ISSN
- 0264-6021
- language
- English
- LU publication?
- yes
- id
- 65380b50-3920-493f-b0e7-36d9ce23c87c (old id 1103691)
- alternative location
- http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1146582&blobtype=pdf
- http://www.biochemj.org/bj/234/0429/2340429.pdf
- date added to LUP
- 2016-04-01 15:48:53
- date last changed
- 2021-04-25 03:31:10
@article{65380b50-3920-493f-b0e7-36d9ce23c87c,
abstract = {{We point out that human low-Mr kininogen contains three cystatin-like sequences, rather than two, as had previously been thought. The protein was purified by affinity chromatography on carboxymethyl-papain-Sepharose, and subjected to limited proteolysis by trypsin and chymotrypsin. Fragments were isolated, and three corresponding to the individual cystatin-like domains were identified. By comparison with the known amino acid sequence of the protein they were numbered 1 to 3 from the N-terminus. Domain 1 was not found to have any inhibitory activity for cysteine proteinases, which is consistent with the absence of residues that are highly conserved in inhibitors of the cystatin superfamily, and have previously been suggested to be essential for activity. Domain 2 was a good inhibitor of chicken calpain, and also papain and cathepsin L. Domain 3 showed negligible inhibition of calpain, but inhibited papain and cathepsin L strongly. The probable arrangement of disulphide bonds in the heavy chain of low-Mr kininogen is deduced from the homology with the cystatins and other evidence contained in the present paper.}},
author = {{Salvesen, Guy and Parkes, Catherine and Abrahamson, Magnus and Grubb, Anders and Barrett, Alan J}},
issn = {{0264-6021}},
language = {{eng}},
number = {{2}},
pages = {{429--434}},
publisher = {{Portland Press}},
series = {{Biochemical Journal}},
title = {{Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases.}},
url = {{http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1146582&blobtype=pdf}},
volume = {{234}},
year = {{1986}},
}