| pubmed-article:6254570 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6254570 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:6254570 | lifeskim:mentions | umls-concept:C0014436 | lld:lifeskim |
| pubmed-article:6254570 | lifeskim:mentions | umls-concept:C1521970 | lld:lifeskim |
| pubmed-article:6254570 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:6254570 | lifeskim:mentions | umls-concept:C1412936 | lld:lifeskim |
| pubmed-article:6254570 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:6254570 | lifeskim:mentions | umls-concept:C0332282 | lld:lifeskim |
| pubmed-article:6254570 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:6254570 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:6254570 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6254570 | pubmed:dateCreated | 1981-2-26 | lld:pubmed |
| pubmed-article:6254570 | pubmed:abstractText | 1. Upon incubation for 1 h at 37 degrees C, proenzymic C1r was activated by a proteolytic cleavage comparable to that observed in vivo; after reduction and alkylation, two fragments of apparent molecular weights 57 000 and 35 000 were evident on sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis. The activation kinetics were slightly sigmoidal and nearly independent of C1r concentration. They were characterized by a marked thermal dependence (activation energy = 45 kcal/mol). The reaction was inhibited by calcium and p-nitrophenyl-p'-guanidinobenzoate, but poorly sensitive to di-isopropyl phosphorofluoridate. The dependence of the activation rate on pH was unusual; it decreased progressively in the acid range (pH 4.5-6.5) which coincides with the dissociation of the C1r-C1r dimer. Above pH 6.5, the rate increased slightly and showed no clear maximum. These results are consistent with an intramolecular autocatalytic activation mechanism involving the pro-site of each subunit of the C1r-C1r dimer. 2. During a 5 h incubation period at 37 degrees C, C1r underwent two proteolytic cleavages which led to the successive removal of two fragments, alpha (35 000) and beta (7000-11 000) from each subunit, leaving a dimeric molecule of reduced size (Mr = 110 000; s20,w = 6.1 S). The proteolytic process was nearly independent of C1r concentration and characterized by a pH optimum at 8.5-9.0, and a high activation energy (36.8 kcal/mol). Calcium and p-nitrophenyl-p'-guanidinobenzoate, and also di-isopropyl phosphorofluoridate and benzamidine were inhibitors of this reaction. The product, C1r II, retained the original antigenic properties of C1r and a functional active site, but lost the capacity to bind C1s. These results are consistent with an autocatalytic intramolecular proteolysis mediated by the active site of each subunit of the C1r-C1r dimer. | lld:pubmed |
| pubmed-article:6254570 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6254570 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6254570 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6254570 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6254570 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6254570 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:6254570 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:6254570 | pubmed:author | pubmed-author:ColombM GMG | lld:pubmed |
| pubmed-article:6254570 | pubmed:author | pubmed-author:ArlaudG JGJ | lld:pubmed |
| pubmed-article:6254570 | pubmed:author | pubmed-author:ChesneSS | lld:pubmed |
| pubmed-article:6254570 | pubmed:author | pubmed-author:VilliersC LCL | lld:pubmed |
| pubmed-article:6254570 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6254570 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:6254570 | pubmed:volume | 616 | lld:pubmed |
| pubmed-article:6254570 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6254570 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6254570 | pubmed:pagination | 116-29 | lld:pubmed |
| pubmed-article:6254570 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:6254570 | pubmed:year | 1980 | lld:pubmed |
| pubmed-article:6254570 | pubmed:articleTitle | Purified proenzyme C1r. Some characteristics of its activation and subsequent proteolytic cleavage. | lld:pubmed |
| pubmed-article:6254570 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6254570 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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