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pubmed-article:8728828pubmed:dateCreated1996-11-7lld:pubmed
pubmed-article:8728828pubmed:abstractTextA second degree equation fitted by nonlinear regression for the analysis of the pH effect on enzyme activity is proposed for diprotic enzyme systems. This method allows the calculation of two molecular dissociation constants (KE1 and KE2 for the free enzyme, KES1 and KES2 for the ES complex) and the pH independent parameters (Vmax and Vmax/Km). The method is validated by bibliographic (alpha-chymotrypsin) and experimental data (almond beta-D-glucosidase). No significant differences were found between present data and those previously reported in the literature using similar experimental conditions. This method works using comparatively few [H+] concentration values within a narrow pH range, preferentially around the optimum, being adequate for diprotic systems with close pKa values.lld:pubmed
pubmed-article:8728828pubmed:languageenglld:pubmed
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pubmed-article:8728828pubmed:statusMEDLINElld:pubmed
pubmed-article:8728828pubmed:issn0716-9760lld:pubmed
pubmed-article:8728828pubmed:authorpubmed-author:O'ReillySSlld:pubmed
pubmed-article:8728828pubmed:authorpubmed-author:RiverosM CMClld:pubmed
pubmed-article:8728828pubmed:issnTypePrintlld:pubmed
pubmed-article:8728828pubmed:volume27lld:pubmed
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pubmed-article:8728828pubmed:pagination171-6lld:pubmed
pubmed-article:8728828pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:8728828pubmed:year1994lld:pubmed
pubmed-article:8728828pubmed:articleTitleDetermination of the pKa of ionizable enzyme groups by nonlinear regression using a second degree equation.lld:pubmed
pubmed-article:8728828pubmed:affiliationFacultad de Ciencias Básicas y Matemáticas, Universidad Católica de Valparaíso, Chile.lld:pubmed
pubmed-article:8728828pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8728828pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed