| Summary: | 碩士 === 東海大學 === 生物學研究所 === 82 === Glutathione S-transferase (GST) which was purified from
Aedesline, C6/36, was treated with tetranitromethane (TNM),
pyridoxal 5-phosphate (PLP) diethylpyrocarbonate (DEPC) andle.
The tyrosine-specific reagent TNM inactivated the enzyme-
hexylglutathione, glutathuonyl 2,4- dinitrobenzene (GSDNB)
andprotected against this inactivation. Binding affinity
forelectrophilic substrates of TNM-treated GS was significantly
greater than those of untreated enzyme. Thesethat tyrosine in
the glutathine binding site (G-site) andng site (H-site) may be
functionally important in catalysis andng. From the same
method, arginine in the G-site and H-site mayimportant in
catalysis and that this residue in the H-site may bebstrate
binding. Lysine in G-site and H-site may not be importantnding
but may be funtionally important in catalysis. The histidine-
specificd cysteine-specific reagent N-acetylimidazole did not
inactivatendicating that histidine and cysteine are not
essential in
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