journal cover

The influence of pH on the interaction of inhibitors with triosephosphate isomerase and determination of the pKa of the active-site carboxyl group

Biochemistry

Dec 2, 1975

F C HartmanR Wolfenden

Abstract

Ionization effects on the binding of the potential transition state analogues 2-phosphoglycolate and 2-phosphoglycolohydroxamate appear to be attributable to the changing state of ionization of the ligands themselves, therefore it is unnecessary to postulate the additional involvement o...read more

Mentioned in this Paper

Hydrogen-Ion Concentration
Hydroxymercuribenzoates
Isomerase
Phosphate ion
Ligands
Muscle
Inorganic phosphate
Plasma Protein Binding Capacity
Saccharomyces cerevisiae
Metazoa
56
2
Paper Details
References
  • References
  • Citations36
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations36
1234

The influence of pH on the interaction of inhibitors with triosephosphate isomerase and determination of the pKa of the active-site carboxyl group

Biochemistry

Dec 2, 1975

F C HartmanR Wolfenden

PMID: 47

DOI: 10.1021/bi00695a007

Abstract

Ionization effects on the binding of the potential transition state analogues 2-phosphoglycolate and 2-phosphoglycolohydroxamate appear to be attributable to the changing state of ionization of the ligands themselves, therefore it is unnecessary to postulate the additional involvement o...read more

Mentioned in this Paper

Hydrogen-Ion Concentration
Hydroxymercuribenzoates
Isomerase
Phosphate ion
Ligands
Muscle
Inorganic phosphate
Plasma Protein Binding Capacity
Saccharomyces cerevisiae
Metazoa
56
2

Related Papers

Paper Details
References
  • References
  • Citations36
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations36
1234
/papers/the-influence-of-ph-on-the-interaction-of/47