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J. Biochem, 1980, Vol. 87, No. 4 1243-1248
© 1980 Japanese Biochemical Society

research-article

Studies on the Structure of {gamma}-Glutamyltranspeptidase

I. Correlation between Sialylation and Isozymic Forms1

Yoshiko MATSUDA, Akihiko TSUJI and Nobuhiko KATUNUMA

Department of Enzyme Chemistry, Institute for Enzyme Research, School of Medicine, Tokushima University Tokushima, Tokushima 770

Papain solubilized {gamma}-glutamyltranspeptidase was purified by DEAE-cellulose column chromatography. Four fractions were obtained as single proteins, each with a single isoelectric point, and fifth and sixth fractions were obtained as mixtures of several components. The molecular weights of the subunits of each form and their amino acid compositions and carboxyl-terminals were determined and found to be identical. The isoelectric points of the four purified enzymes and the main bands of the fifth fraction were pH 8.3, 8.0, 7.5, 6.7, and 6.0, respectively. The sixth fraction gave five bands with isoelectric points of pH 5.6, 5.3, 5.1, 4.6, and 4.4. An asialo-form of the enzyme, obtained by treatment with neuraminidase, had an isoelectric point of pH 8.6. A linear relationship was found between the isoelectric points of the enzymes and their contents of sialic acid, indicating that the heterogeneity of papain-solubilized {gamma}-glutamyltranspeptidase is mostly due to differences in the extents of sialylation of the enzymes. The distribution of the activity in rat kidney was as follows: 29% in a poorly sialylated fraction (isoelectric point (Ip) 8.3 to 6.7), 24% in a moderately sialylated fraction (Ip 6.6 to 6.0), and 45% in a highly sialylated fraction (Ip 5.6 to 4.4).

1 This study was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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