pubmed-article:238943 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:238943 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:238943 | lifeskim:mentions | umls-concept:C1440044 | lld:lifeskim |
pubmed-article:238943 | lifeskim:mentions | umls-concept:C0872306 | lld:lifeskim |
pubmed-article:238943 | lifeskim:mentions | umls-concept:C0285969 | lld:lifeskim |
pubmed-article:238943 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:238943 | pubmed:dateCreated | 1975-11-6 | lld:pubmed |
pubmed-article:238943 | pubmed:abstractText | Baker's yeast was found to contain inhibitors of yeast proteases A and C. These two proteins were partially purified, characterized, and compared with the previously described inhibitor of protease B. The A and B inhibitors were very thermostable and were extracted from intact yeast cells at 9k C. The A inhibitor appeared to be a protein with a molecular weight of about 22,000 which could be dissociated into two monomers or chains, both of which had a molecular weight of approximately 11,000. The protease C (carboxypeptidase Y)-inhibitor complex was purified and then partially disociated on an ion-exchange column. The free protease C inhibitor was very unstable, possibly because of destruction by a contaminating protease. Each inhibitor was specific for its corresponding protease and each inhibition was competitive. Whereas proteases A, B, and C destroyed the B inhibitor, only protease B had a pronounced destructive effect on the protease A inhibitor. Pepstatin was found to be a selective inhibitor of protease A, whereas chymostatin and antipain specifically inhibited protease B. | lld:pubmed |
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pubmed-article:238943 | pubmed:language | eng | lld:pubmed |
pubmed-article:238943 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:238943 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:238943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:238943 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:238943 | pubmed:month | Jun | lld:pubmed |
pubmed-article:238943 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:238943 | pubmed:author | pubmed-author:LenneyJ FJF | lld:pubmed |
pubmed-article:238943 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:238943 | pubmed:volume | 122 | lld:pubmed |
pubmed-article:238943 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:238943 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:238943 | pubmed:pagination | 1265-73 | lld:pubmed |
pubmed-article:238943 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:238943 | pubmed:year | 1975 | lld:pubmed |
pubmed-article:238943 | pubmed:articleTitle | Three yeast proteins that specifically inhibit yeast proteases A, B, and C. | lld:pubmed |
pubmed-article:238943 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:238943 | pubmed:publicationType | Comparative Study | lld:pubmed |
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