Purification and properties of gamma-glutamyl transpeptidase from human testis.

Abstract:

:Gamma-glutamyl transpeptidase was purified to apparent homogeneity from human testis by DEAE cellulose, acetone, precipitation, fractionation by ammonium sulphate, Sephacryl S-200 chromatography, Q-Sepharose chromatography and S-Sepharose chromatography following solubilization of the enzyme by Triton X-100. The purified enzyme had an apparent molecular weight of 54 KDa by Sephacryl S-200 gel filtration. On sodium dodecyl sulphate polyacrylamide gel electrophoresis, two submits of molecular weight 38 KDa and 14 KDa were obtained. The purified enzyme showed a single band with pI 6.0. The Km value and the optimal pH of the enzyme for L-gamma-glutamyl-3-carboxy-4-nitroanilide were found 1.09 mmol/l and 8.2-8.5, respectively. Serial lectin binding study with various lectin columns showed that the majority of the asparagine-linked oligosaccharides of the enzyme was complex-types. However, complex-types with bisecting N-acetylglucosamine residue were not recognized.

journal_name

Andrologia

journal_title

Andrologia

authors

Yoshida K,Arai K,Kobayashi N,Saitoh H

doi

10.1111/j.1439-0272.1990.tb01973.x

subject

Has Abstract

pub_date

1990-05-01 00:00:00

pages

239-46

issue

3

eissn

0303-4569

issn

1439-0272

journal_volume

22

pub_type

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