GTPase and transglutaminase are associated in the secretion of the rat anterior prostate.
We have found that in the secretion of rat anterior prostate, a hydrolyzing activity on GTP is present with a high affinity for the substrate; ATP, GDP, and ADP are not substrates for enzymatic activity. At the same time we have shown that GTP is a negative modulator for the well-known type IV transglutaminase activity present in the prostatic secretion. The hydrolyzing activity on GTP appears to be due to two molecular species: a high-molecular-weight GTPase, having electrophoretical mobility higher than 100 kDa, and a low-molecular-weight GTPase, of about 30 kDa. The two enzymatic activities are associated in the prostatic secretion with the transglutaminase (type IV). We describe an experimental procedure to separate them.
Spina
A M
AM
Department of Biochemistry and Biophysics, 2nd University of Naples, via Costantinopoli 16, Naples, 80138, Italy.
Esposito
C
C
Pagano
M
M
Chiosi
E
E
Mariniello
L
L
Cozzolino
A
A
Porta
R
R
Illiano
G
G
D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D008297:Male; D008970:Molecular Weight; D011467:Prostate / Q000201:enzymology / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D011503:Transglutaminases / Q000302:isolation & purification / Q000378:metabolism*
D006160:Guanosine Triphosphate; D011503:Transglutaminases; D020558:GTP Phosphohydrolases