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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)
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in
Biochemical Journal
volume
234
issue
2
pages
429 - 434
publisher
Portland Press Limited
ISSN
0264-6021
language
English
LU publication?
yes
id
65380b50-3920-493f-b0e7-36d9ce23c87c (old id 1103691)
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http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1146582&blobtype=pdf
http://www.biochemj.org/bj/234/0429/2340429.pdf
date added to LUP
2008-08-11 11:08:22
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2016-04-16 03:23:10
@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 Limited},
  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.},
  volume       = {234},
  year         = {1986},
}