rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
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pubmed:dateCreated |
1985-4-19
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pubmed:abstractText |
Cathepsin L was purified to apparent homogeneity from human liver obtained post mortem. It was necessary to treat the homogenate at pH 4.2 and 37 degrees C to release active enzyme. The purification procedure involved ion-exchange chromatography on carboxymethyl-Sephadex and the Mono S column of a Pharmacia fast-protein-liquid-chromatography system. The enzyme was found to consist of two polypeptide chains of Mr 25 000 and 5000. The larger chain was shown to contain the active-site cysteine residue. Human cathepsin L proved to be similar to the rat and rabbit enzymes in regard to kinetic constants for the substrate benzyloxycarbonylphenylalanylarginine 7-(4-methyl)coumarylamide and rates of inactivation by the active-site-directed reagents benzyloxycarbonylphenylalanylphenylalanyldiazomethane and benzyloxycarbonylphenylalanylalanyldiazomethane. Thus clear characteristics of cathepsin L are now emerging, and these should simplify the identification of the enzyme in other tissues and species.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-13785321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-15835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-399887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-4263188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-4734223,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-4940753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-6165352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-627216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-6421281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-6424735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-6426465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-6429090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-6468652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-6547604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-6548132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-6754441,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-7043200,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/3977867-942051
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Feb
|
pubmed:issn |
0264-6021
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
|
pubmed:volume |
226
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
233-41
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:3977867-Cathepsin B,
pubmed-meshheading:3977867-Cathepsin L,
pubmed-meshheading:3977867-Cathepsins,
pubmed-meshheading:3977867-Chromatography, Ion Exchange,
pubmed-meshheading:3977867-Cysteine Endopeptidases,
pubmed-meshheading:3977867-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3977867-Endopeptidases,
pubmed-meshheading:3977867-Humans,
pubmed-meshheading:3977867-Kinetics,
pubmed-meshheading:3977867-Liver,
pubmed-meshheading:3977867-Molecular Weight,
pubmed-meshheading:3977867-Peptides,
pubmed-meshheading:3977867-Substrate Specificity
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pubmed:year |
1985
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pubmed:articleTitle |
Human liver cathepsin L.
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pubmed:publicationType |
Journal Article
|