Resistance to inactivation by EGTA of the enzyme-substrate and enzyme-phosphate complexes of alkaline phosphatase.

Pike S.J. and Duggleby R.G. (1987) Resistance to inactivation by EGTA of the enzyme-substrate and enzyme-phosphate complexes of alkaline phosphatase.. Biochemical Journal, 244 3: 781-785. doi:10.1042/bj2440781


Author Pike S.J.
Duggleby R.G.
Title Resistance to inactivation by EGTA of the enzyme-substrate and enzyme-phosphate complexes of alkaline phosphatase.
Journal name Biochemical Journal   Check publisher's open access policy
ISSN 0264-6021
Publication date 1987-06-15
Sub-type Article (original research)
DOI 10.1042/bj2440781
Open Access Status Not yet assessed
Volume 244
Issue 3
Start page 781
End page 785
Total pages 5
Language eng
Subject 1303 Specialist Studies in Education
Abstract Bovine intestinal mucosal alkaline phosphatase is inactivated by the chelating agent EGTA. Several concentrations of the enzyme were incubated with EGTA and a range of concentrations of the substrate p-nitrophenyl phosphate to determine the substrate concentration as a function of time. As predicted by a recently developed theory [Duggleby (1986) J. Theor. Biol. 123, 67-80], catalysis ceases before all substrate is exhausted. An analysis of these final substrate concentrations according to the theory revealed that, whereas the free enzyme is unstable, the effect of EGTA is counteracted when either the substrate or product (phosphate) is bound. Comparison of the results with those obtained by direct stability measurements and steady-state kinetic experiments gave a qualitatively and quantitatively consistent body of evidence in support of this interpretation.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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