pubmed-article:6311982 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6311982 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
pubmed-article:6311982 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
pubmed-article:6311982 | lifeskim:mentions | umls-concept:C0086045 | lld:lifeskim |
pubmed-article:6311982 | lifeskim:mentions | umls-concept:C0010661 | lld:lifeskim |
pubmed-article:6311982 | lifeskim:mentions | umls-concept:C0439300 | lld:lifeskim |
pubmed-article:6311982 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:6311982 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:6311982 | lifeskim:mentions | umls-concept:C0006785 | lld:lifeskim |
pubmed-article:6311982 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:6311982 | pubmed:dateCreated | 1983-11-23 | lld:pubmed |
pubmed-article:6311982 | pubmed:abstractText | Synaptosomal plasma membranes (SPMs) were prepared from whole rat brain and assayed for calcium-stimulated proteolytic activity. Addition of calcium to SPMs caused a dose-dependent increase in trichloroacetic acid-soluble protein. Two peaks of protease activity directed against a casein substrate were detectable when SPMs were incubated with low-ionic-strength buffer and the extract was fractionated on DEAE-cellulose. The enzyme in peak 1 required less than 1/10 the calcium concentration for activation as the peak 2 protease (Kact1 = 35 microM; Kact2 = 500 microM). The specific thiol-protease inhibitors leupeptin and antipain and the alkylator iodoacetate blocked enzyme activity. The low-sensitivity protease was converted to a high-sensitivity enzyme (Kact = 20 microM) by substrate affinity chromatography in the presence of calcium. This protease was purified 550-fold from SPMs. The high- and low-sensitivity membrane-associated calcium-dependent proteases are part of a family of enzymes, the calpains, previously reported in cytosolic fractions of several tissues. | lld:pubmed |
pubmed-article:6311982 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6311982 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6311982 | pubmed:language | eng | lld:pubmed |
pubmed-article:6311982 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6311982 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:6311982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6311982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:6311982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6311982 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6311982 | pubmed:month | Oct | lld:pubmed |
pubmed-article:6311982 | pubmed:issn | 0022-3042 | lld:pubmed |
pubmed-article:6311982 | pubmed:author | pubmed-author:BaudryMM | lld:pubmed |
pubmed-article:6311982 | pubmed:author | pubmed-author:LynchGG | lld:pubmed |
pubmed-article:6311982 | pubmed:author | pubmed-author:SimanRR | lld:pubmed |
pubmed-article:6311982 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6311982 | pubmed:volume | 41 | lld:pubmed |
pubmed-article:6311982 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6311982 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6311982 | pubmed:pagination | 950-6 | lld:pubmed |
pubmed-article:6311982 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:6311982 | pubmed:year | 1983 | lld:pubmed |
pubmed-article:6311982 | pubmed:articleTitle | Purification from synaptosomal plasma membranes of calpain I, a thiol protease activated by micromolar calcium concentrations. | lld:pubmed |
pubmed-article:6311982 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:6311982 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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