| pubmed-article:1546965 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1546965 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:1546965 | lifeskim:mentions | umls-concept:C0007589 | lld:lifeskim |
| pubmed-article:1546965 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:1546965 | lifeskim:mentions | umls-concept:C1261552 | lld:lifeskim |
| pubmed-article:1546965 | lifeskim:mentions | umls-concept:C1511938 | lld:lifeskim |
| pubmed-article:1546965 | pubmed:dateCreated | 1992-4-16 | lld:pubmed |
| pubmed-article:1546965 | pubmed:abstractText | It has been suggested that the complexing type of inactivation in which the inactivator binds reversibly with the enzyme before inactivation cannot be differentiated kinetically from that a slow enzyme conformation change is involved as a first step [Rakitzis (1986) J. Theor. Biol. 122, 247-249]. The kinetics of the substrate reaction during modification of enzyme activity previously described [Tsou (1988) Adv. Enzymol. Relat. Areas Mol. Biol. 61, 381-436] have now been applied to this problem and equations derived to show that the slow-conformational-change type can be differentiated from the complexing type by plotting the final concentration of product formed, [P]infinity, against the reciprocal of inactivator concentration. The reaction of hexokinase with 2-chloromercuri-4-nitrophenol has been shown to involve a conformational change of the enzyme before inactivation. | lld:pubmed |
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| pubmed-article:1546965 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1546965 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1546965 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1546965 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1546965 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1546965 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1546965 | pubmed:author | pubmed-author:LisMM | lld:pubmed |
| pubmed-article:1546965 | pubmed:author | pubmed-author:TsouC LCL | lld:pubmed |
| pubmed-article:1546965 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1546965 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1546965 | pubmed:volume | 282 ( Pt 2) | lld:pubmed |
| pubmed-article:1546965 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1546965 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1546965 | pubmed:pagination | 501-4 | lld:pubmed |
| pubmed-article:1546965 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1546965 | pubmed:meshHeading | pubmed-meshheading:1546965-... | lld:pubmed |
| pubmed-article:1546965 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1546965 | pubmed:articleTitle | Kinetic differentiation between enzyme inactivation involving complex-formation with the inactivator and that involving a conformation-change step. | lld:pubmed |
| pubmed-article:1546965 | pubmed:affiliation | National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, People's Republic of China. | lld:pubmed |
| pubmed-article:1546965 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1546965 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1546965 | lld:pubmed |
