Difference in the sugar chains of two subunits and of isozymic forms of rat kidney gamma-glutamyltranspeptidase |
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| Authors: | K Yamashita Y Tachibana A Hitoi Y Matsuda A Tsuji N Katunuma A Kobata |
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| Institution: | 1. Department of Enzyme Chemistry, Institute for Enzyme Research, School of Medicine, Tokushima University, Tokushima, Japan;2. Department of Biochemistry, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo 108, Japan |
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| Abstract: | A comparative study by gel-permeation chromatographic analysis of oligosaccharides released from the heavy and the light subunits of rat kidney gamma-glutamyltranspeptidase has revealed that high-mannose-type sugar chains are found only in the heavy subunit, and the nonsialylated and nonfucosylated biantennary complex-type sugar chains are included only in the light subunit. By the same analysis of the oligosaccharide fractions obtained from four isozymic forms of rat kidney gamma-glutamyltranspeptidase, it was found that all these enzymes contain 2 mol of neutral sugar chains but different numbers of acidic sugar chains. The total numbers of sialic acid residues showed a reciprocal relationship to the isoelectric point of each isozymic form, and an increase of 1 mol of sialic acid residue corresponds to a decrease of 0.5 in the value of the isoelectric point. |
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| Keywords: | To whom correspondence should be addressed |
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