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Sökning: L773:0264 6021 > (1980-1989) > Barrett Alan J > Human low-Mr kinino...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003067naa a2200313 4500
001oai:lup.lub.lu.se:65380b50-3920-493f-b0e7-36d9ce23c87c
003SwePub
008160401s1986 | |||||||||||000 ||eng|
024a https://lup.lub.lu.se/record/11036912 URI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
100a Salvesen, Guy4 aut
2451 0a Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases.
264 1c 1986
520 a 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.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
700a Parkes, Catherine4 aut
700a Abrahamson, Magnusu Lund University,Lunds universitet,Avdelningen för klinisk kemi och farmakologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Clinical Chemistry and Pharmacology,Department of Laboratory Medicine,Faculty of Medicine4 aut0 (Swepub:lu)kkem-mab
700a Grubb, Andersu Lund University,Lunds universitet,Avdelningen för klinisk kemi och farmakologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Clinical Chemistry and Pharmacology,Department of Laboratory Medicine,Faculty of Medicine4 aut0 (Swepub:lu)kkem-agr
700a Barrett, Alan J4 aut
710a Avdelningen för klinisk kemi och farmakologib Institutionen för laboratoriemedicin4 org
773t Biochemical Journalg 234:2, s. 429-434q 234:2<429-434x 0264-6021
856u http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1146582&blobtype=pdfx freey FULLTEXT
856u http://www.biochemj.org/bj/234/0429/2340429.pdfx freey FULLTEXT
8564 8u https://lup.lub.lu.se/record/1103691

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