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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1992-4-16
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-1120099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-1237313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-14033211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-2146263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-2161846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-2162964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-2514790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-2707265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-2713358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-2948570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-3167034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-3281419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-3639874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-3796015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-3863616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-3955054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-4005269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-4314229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-4343169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-4877056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-4985619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-4994927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-6096140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-6782185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1546965-7074045
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
282 ( Pt 2)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
501-4
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
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pubmed:year |
1992
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pubmed:articleTitle |
Kinetic differentiation between enzyme inactivation involving complex-formation with the inactivator and that involving a conformation-change step.
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pubmed:affiliation |
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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