DEGRADATION OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE INTO ENZYMATICALLY ACTIVE MOLECULAR FORMS BY TRYPSIN | Zendy

Samuel H. Hori | Zendy; Setsuko Noda | Zendy

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DEGRADATION OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE INTO ENZYMATICALLY ACTIVE MOLECULAR FORMS BY TRYPSIN

Author(s) -

Samuel H. Hori,

Setsuko Noda

Publication year - 1971

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.971

H-Index - 124

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/19.5.299

Subject(s) - isozyme , biochemistry , trypsin , enzyme , glucose 6 phosphate dehydrogenase , dehydrogenase , chemistry , substrate (aquarium) , electrophoresis , phosphate , substrate specificity , degradation (telecommunications) , digestion (alchemy) , biology , chromatography , ecology , telecommunications , computer science

One of the hepatic glucose 6-phosphate dehydrogenase isozymes of rats, designated "C," has been degraded by tryptic digestion into two enzymatically active forms of different electrophoretic mobility. The modified forms exhibited the same substrate specificity and mobility as the isozymes previously designated E and E'. The results of the present study emphasized that zymograms of tissues rich in proteinases should be interpreted with caution.

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