[Guanyl cyclase in Escherichia coli. II. Identification and characteristics on the enzyme inhibitor].
The activity of guanylate cyclase and that of its inhibitor present in E. coli extract, have been separated through a linear KCl gradient on DEAE-cellulose column. The activity of the inhibitor is lost after ribonuclease treatment, whereas is strengthened by addition of poly (C). Other types of RNA synthetic homopolymers do not affect the inhibitor's activity. Chromatographic analysis of the products of guanylate cyclase measured in the presence of FI and FI plus poly (C), indicated that the inhibitor has a poly (C) dependent GTPase activity.
D003851:Deoxyribonucleases; D004926:Escherichia coli / Q000201:enzymology*; D020558:GTP Phosphohydrolases / Q000302:isolation & purification* / Q000378:metabolism; D006162:Guanylate Cyclase / Q000037:antagonists & inhibitors*; D007700:Kinetics; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification*; D011066:Poly C / Q000494:pharmacology; D012260:Ribonucleases; D014357:Trypsin
D011066:Poly C; D003851:Deoxyribonucleases; D012260:Ribonucleases; D010744:Phosphoric Monoester Hydrolases; D014357:Trypsin; D020558:GTP Phosphohydrolases; D006162:Guanylate Cyclase
Guanylate cyclase chez Escherichia coli. II. Identification et caractéristiques d'un inhibiteur de l'enzyme.