Guanylate cyclase in E. coli. III. Purification and possible physiological role of GTPase
Rocino, A.; Macchia, V.; Gulletta, E.; Consiglio, E.; Varrone, S.
Comptes Rendus des Seances de la Societe de Biologie et de ses Filiales 172(6): 1079-1084
1978
ISSN/ISBN: 0037-9026 PMID: 40673 Document Number: 126187
A phosphohydrolase with a preferential activity for GTP has been isolated and partially purified from E. coli extracts. The enzyme purification has been achieved through precipitation by ammonium sulfate and chromatography on DEAE-cellulose, DEAE-Sephadex, Ultragel and a second DEAE-cellulose column. The phosphohydrolase activity is poly (C) dependent. The chromatographic analysis on PEI-cellulose has shown that the main product of GTP hydrolysis is GDP. The possibility that the enzyme partially purified in this work has an important role in the control of GTP availability as substrate for guanylate cyclase into the cells has been discussed.