Identification and partial purification of a nucleotide-stimulated protease in rat retina.
A nucleotide-stimulated protease of rat retina was partially purified by DEAE-cellulose column chromatography. A 50-fold increase of an ATP-stimulated protease activity over a cytosol fraction was achieved by this chromatography. Maximum stimulation of protease activity by ATP was achieved at 2 mM. The pH optimum of the ATP-stimulated protease activity was between 7.5 and 8.5. 2 mM GTP stimulated the protease activity by 91%. 5 mM cyclic AMP stimulated the protease activity by 73% while 5 mM cyclic GMP stimulated the activity by 84%. The possible role of the nucleotide-stimulated protease in retina and potential involvement of the protease with inherited retinal dystrophy are discussed.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D006152:Cyclic GMP / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D012160:Retina / Q000201:enzymology*
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D010447:Peptide Hydrolases; D006152:Cyclic GMP