| pubmed-article:6282261 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C0009498 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C1412936 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C0486805 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C1706793 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C0056658 | lld:lifeskim |
| pubmed-article:6282261 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
| pubmed-article:6282261 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6282261 | pubmed:dateCreated | 1982-7-8 | lld:pubmed |
| pubmed-article:6282261 | pubmed:abstractText | 1. The a- and b-chains of reduced and alkylated human complement subcomponent C1r were separated by high-pressure gel-permeation chromatography and isolated in good yield and in pure form. 2. CNBr cleavage of C1r b-chain yielded eight major peptides, which were purified by gel filtration and high-pressure reversed-phase chromatography. As determined from the sum of their amino acid compositions, these peptides accounted for a minimum molecular weight of 28 000, close to the value 29 100 calculated from the whole b-chain. 3. N-Terminal sequence determinations of C1r b-chain and its CNBr-cleavage peptides allowed the identification of about two-thirds of the amino acids of C1r b-chain. From our results, and on the basis of homology with other serine proteinases, an alignment of the eight CNBr-cleavage peptides from C1r b-chain is proposed. 4. The residues forming the 'charge-relay' system of the active site of serine proteinases (His-57, Asp-102 and Ser-195 in the chymotrypsinogen numbering) are found in the corresponding regions of C1r b-chain, and the amino acid sequence around these residues has been determined. 5. The N-terminal sequence of C1r b-chain has been extended to residue 60 and reveals that C1r b-chain lacks the 'histidine loop', a disulphide bond that is present in all other known serine proteinases. | lld:pubmed |
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| pubmed-article:6282261 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6282261 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6282261 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6282261 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:6282261 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6282261 | pubmed:author | pubmed-author:ArlaudG JGJ | lld:pubmed |
| pubmed-article:6282261 | pubmed:author | pubmed-author:GagnonJJ | lld:pubmed |
| pubmed-article:6282261 | pubmed:author | pubmed-author:PorterR RRR | lld:pubmed |
| pubmed-article:6282261 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6282261 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:6282261 | pubmed:volume | 201 | lld:pubmed |
| pubmed-article:6282261 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6282261 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6282261 | pubmed:pagination | 49-59 | lld:pubmed |
| pubmed-article:6282261 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6282261 | pubmed:year | 1982 | lld:pubmed |
| pubmed-article:6282261 | pubmed:articleTitle | The catalytic chain of human complement subcomponent C1r. Purification and N-terminal amino acid sequences of the major cyanogen bromide-cleavage fragments. | lld:pubmed |
| pubmed-article:6282261 | pubmed:publicationType | Journal Article | lld:pubmed |
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