Physiochemical and Immunochemical Characterization of Gamma-glutamyl Transpeptidase from Yolk Sak Tumor and Ascitic Hepatoma (AH-66) Cells
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gamma-Glutamyl transpeptidases, purified from rat yolk sac tumor and AH-66 hepatoma cell lines resemble this enzyme system from rat kidney in their amino acid composition and antigenicity, but differ by having a higher carbohydrate content. The different carbohydrate contents resulted in the tumor cell and rat kidney enzymes having different molecular weights. Isoelectric focusing of the neuraminidase-treated enzymes showed that a substantial portion of the enzymes from yolk sac tumor and AH-66 cells shifted to a form with an isoelectric point at pH 7.4. However, a heterogeneous pattern was still found in the kidney enzyme even after extensive neuraminidase treatment.
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