| pubmed-article:7864827 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0008736 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0010646 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0439659 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C1441672 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0008550 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C1511539 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C2700116 | lld:lifeskim |
| pubmed-article:7864827 | lifeskim:mentions | umls-concept:C0050639 | lld:lifeskim |
| pubmed-article:7864827 | pubmed:dateCreated | 1995-3-21 | lld:pubmed |
| pubmed-article:7864827 | pubmed:abstractText | 1. The selectivity observed when the potentially general technique for the isolation of fully active forms of cysteine proteinases, covalent chromatography by thiol-disulphide interchange, is applied to chymopapain M and to actinidin was investigated by a combination of experimentation and computer modelling. Neither of these enzymes is able to react with the original Sepharose-GSH-2-dipyridyl disulphide gel, but fully active forms of both enzymes are obtained by using Sepharose-2-hydroxypropyl-2'-dipyridyl disulphide gel, which is both electrically neutral and sterically less demanding than the GSH gel. Electrostatic potential calculations, minimization and molecular-dynamics simulations provide explanations for the unusual, but different, specificities exhibited by actinidin and chymopapain M in the interactions of their active centres with ligands. 2. The unique behaviour of chymopapain M in exerting an almost absolute specificity for substrates with glycine at the P1 position and in resisting inhibition by cystatin was examined by the computer-modelling techniques. A new, modelled, structure of the complete chicken egg-white cystatin molecule based on the crystal structure of a short form of cystatin was deduced as a necessary prerequisite. The results suggest that electrostatic repulsion prevents reaction of actinidin with the GSH gel, whereas a steric 'cap' resulting from a unique arginine-65-glutamic acid-23 interaction in chymopapain M prevents reaction of the gel with this enzyme and accounts for the lack of its inhibition by cystatin and its specificity in catalysis. 3. Use of chymopapain M as a structural variant of papain demonstrates the validity of the predictions of Lowe and Yuthavong [Biochem. J. (1971) 124, 107-115] relating to the structural requirements and binding characteristics of the S1 subsite of papain. | lld:pubmed |
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| pubmed-article:7864827 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7864827 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7864827 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7864827 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:7864827 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7864827 | pubmed:author | pubmed-author:BrocklehurstK... | lld:pubmed |
| pubmed-article:7864827 | pubmed:author | pubmed-author:ThomasM PMP | lld:pubmed |
| pubmed-article:7864827 | pubmed:author | pubmed-author:VermaCC | lld:pubmed |
| pubmed-article:7864827 | pubmed:author | pubmed-author:BomeM PMP | lld:pubmed |
| pubmed-article:7864827 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7864827 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7864827 | pubmed:volume | 306 ( Pt 1) | lld:pubmed |
| pubmed-article:7864827 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7864827 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7864827 | pubmed:pagination | 39-46 | lld:pubmed |
| pubmed-article:7864827 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7864827 | pubmed:meshHeading | pubmed-meshheading:7864827-... | lld:pubmed |
| pubmed-article:7864827 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7864827 | pubmed:articleTitle | The structural origins of the unusual specificities observed in the isolation of chymopapain M and actinidin by covalent chromatography and the lack of inhibition of chymopapain M by cystatin. | lld:pubmed |
| pubmed-article:7864827 | pubmed:affiliation | Department of Biochemistry, Queen Mary and Westfield College, University of London, U.K. | lld:pubmed |
| pubmed-article:7864827 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7864827 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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