Changes in the kinetic parameters of hepatic γ-glutamyltransferase from streptozotocin-induced diabetic rats

Paul D. Cornwell, John B. Watkins

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Previous research has shown that the enzymatic activity of hepatic γ-glutamyltransferase was increased in streptozotocin-induced diabetic rats with no increase in the expression of the protein. The current work has characterized the differences in the kinetic properties of hepatic γ-glutamyltransferase from diabetic versus control rats. Hepatic γ-glutamyltransferase was purified from control male and female rats and from rats made diabetic 30 days previously with streptozotocin. The maximal velocity and the Michaelis constant were determined for the purified enzyme with two separate donors (L-γ-glutamyl-p-nitroanilide or L-γ-glutamyl-(7-amido-4-methylcoumarin)) in the presence of one of eight acceptors (L-alanine-glycine, L-glycine-glycine, L-methionine, L-glutamate, L-alanine, L-glutamine, L-phenylalanine or L-aspartate). With both donors, hepatic γ-glutamyltransferase from diabetic rats had a consistently higher kinetic efficiency than γ-glutamyltransferase from controls. The kinetic efficiency percent increase of diabetic over control γ-glutamyltransferase when averaged across all acceptors was higher in males than in females. With L-γ-glutamyl-p-nitroanilide, the kinetic efficiency increase of diabetic over control γ-glutamyltransferase was higher with poor acceptors than with highly efficient acceptors. These data indicate that there are differences in the physical properties of hepatic γ-glutamyltransferase from diabetic versus control rats and from female versus male rats.

Original languageEnglish
Pages (from-to)184-191
Number of pages8
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1545
Issue number1-2
DOIs
StatePublished - Feb 9 2001

Fingerprint

Streptozocin
Kinetic parameters
Rats
Rat control
Liver
Kinetics
Glycine
alanylglycine
Glutamine
Phenylalanine
Aspartic Acid
Alanine
Methionine
Glutamic Acid
Physical properties
Enzymes
Proteins
Research

Keywords

  • γ-Glutamyltransferase
  • Diabetes mellitus
  • Enzyme kinetics
  • Glycosidase
  • Glycosyltransferase
  • Streptozotocin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • Biophysics

Cite this

Changes in the kinetic parameters of hepatic γ-glutamyltransferase from streptozotocin-induced diabetic rats. / Cornwell, Paul D.; Watkins, John B.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1545, No. 1-2, 09.02.2001, p. 184-191.

Research output: Contribution to journalArticle

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