Biochemical and immunologic studies on the native and deglycosylated forms of gamma-glutamyltranspeptidase of rat kidney.
We have deglycosylated the enzyme gamma-glutamyl transpeptidase by treatment of the protein with anhydrous hydrofluoric acid at 0 degree C. After deglycosylation, the heavy and light subunits showed a molecular weight of 43 and 23 Kd respectively. Whereas the antiserum against the native enzyme recognized both proteins, the antiserum against the deglycosylated enzyme failed to recognize the native enzyme, indicating that some of the determinants of the native enzyme are masked by the carbohydrate moiety.
Coloma
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Pitot
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D000818:Animals; D006023:Glycoproteins / Q000276:immunology*; D007668:Kidney / Q000201:enzymology*; D008970:Molecular Weight; D051381:Rats; D013329:Structure-Activity Relationship; D005723:gamma-Glutamyltransferase / Q000276:immunology*
D006023:Glycoproteins; D005723:gamma-Glutamyltransferase