Characteristics of the inhibition of poly(ADP-ribose) glycohydrolase by homopolypurines.
Poly(ADP-ribose) glycohydrolase partially purified from rat testis was markedly inhibited by the homopolypurines polyG, polyI and polyA. The inhibition was competitive with respect to poly(ADP-ribose) and the Ki for polyG and polyA was 2.8 uM and 5.5 uM, respectively. This inhibitory effect of the homopolypurines was practically eliminated when 250 mM KCl was present in the reaction mixture. Moreover, the inhibition exerted by polyI or polyA was markedly diminished after hybridization with polyC or polyT, respectively.
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Instituto de Bioquimica, Facultad de Ciencias, Universidad Austral de Chile, Valdivia.
Koide
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Burzio
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D000818:Animals; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D007700:Kinetics; D008297:Male; D011061:Poly A / Q000494:pharmacology*; D011066:Poly C / Q000494:pharmacology; D011068:Poly G / Q000494:pharmacology*; D011069:Poly I / Q000494:pharmacology*; D011071:Poly T / Q000494:pharmacology; D011131:Polyribonucleotides / Q000494:pharmacology*; D051381:Rats; D013737:Testis / Q000201:enzymology*
D011131:Polyribonucleotides; D011061:Poly A; D011071:Poly T; D011068:Poly G; D011069:Poly I; D011066:Poly C; D006026:Glycoside Hydrolases; C022407:poly ADP-ribose glycohydrolase