Abstract
1. 1. Limited proteolyzed glutamate dehydrogenase (GDH) was purified from acetone powder prepared from fresh eel livers. 2. 2. The limited proteolyzed GDH has a subunit of 50,000 molecular weight as well as a subunit of 54,000 molecular weight, and the specific activity of the GDH was higher than that of the native GDH. 3. 3. The amino acid composition and sequence of four residues from the N- terminal of the limited proteolyzed GDH were the same as those of the trypsin-treated GDH (Tang et al., J. Biochem. 111, 655–661, 1992). 4. 4. Effects of PCMB, ADP and GTP on the limited proteolyzed GDH were comparable with those on the trypsin-treated GDH. 5. 5. Proteases extracted from the acetone powder of the fresh livers were applied to a typsin inhibitor-Sepharose column, and proteases retained on this column did not bring about limited proteolysis of the native GDH.
Published Version
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