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pubmed-article:2634098pubmed:abstractTextOrdinary tight-binding inhibition in steady-state enzyme systems is conveniently evaluated by means of the Henderson plot. This is a linear plotting form that has an ordinate intercept equal to the total enzyme concentration. However, there are two experimental situations that yield deviations from the common Henderson plot form. These are inhibitor binding in a separate, noninhibitory mode that depletes the concentration of free inhibitor, and partial inhibition, i.e., the retention of partial activity by the enzyme-inhibitor complex. Noninhibitory depletion results in Henderson plots with elevated ordinate intercepts. Competitive partial inhibition yields a characteristic pattern of parabolic Henderson plots.lld:pubmed
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pubmed-article:2634098pubmed:authorpubmed-author:WestleyJJlld:pubmed
pubmed-article:2634098pubmed:authorpubmed-author:JarabakRRlld:pubmed
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pubmed-article:2634098pubmed:pagination263-5lld:pubmed
pubmed-article:2634098pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:2634098pubmed:year1989lld:pubmed
pubmed-article:2634098pubmed:articleTitleAppendix to the sulfur-cyanolysis sites of serum albumin: metabolite competition studies. Tight-binding inhibitions that yield atypical Henderson plots.lld:pubmed
pubmed-article:2634098pubmed:affiliationDepartment of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637.lld:pubmed
pubmed-article:2634098pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2634098pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed