title: Purified retinal nitric oxide synthase enhances ADP-ribosylation of rod outer segment proteins.
abstract: Nitric oxide synthase is present in different cell layers of vertebrate retina and seems to have neuromodulatory functions in the outer retina. The enzyme, when purified from a bovine retina extract, has an apparent molecular mass of 160 kDa and resembles the neuronal constitutive NOS type I with respect to Ca(2+)-calmodulin sensitivity, Km value and inhibition by analogues of L-arginine. Retinal NOS is present in a preparation of rod outer segments attached to parts of the inner segments, but not in pure outer segments. We describe the enhancement of specific ADP-ribosylation of outer segment proteins by purified retinal NOS.
authors.affiliation: Institut für Biologische Informationsverarbeitung, Forschungszentrum Jülich, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Zoche
authors.forename: K W
authors.initials: KW
authors.lastname: Koch
mesh_terms: D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000594:Amino Acid Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D004789:Enzyme Activation; D005136:Eye Proteins / Q000378:metabolism*; D019001:Nitric Oxide Synthase; D012160:Retina / Q000201:enzymology*; D012374:Rod Cell Outer Segment / Q000378:metabolism*
chemical_list: D005136:Eye Proteins; D000246:Adenosine Diphosphate Ribose; D019001:Nitric Oxide Synthase; D000594:Amino Acid Oxidoreductases