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Purified retinal nitric oxide synthase enhances ADP‐ribosylation of rod outer segment proteins
Author(s) -
Zoche Martin,
Koch Karl-Wilhelm
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01355-5
Subject(s) - nitric oxide synthase , retina , retinal , visual phototransduction , calmodulin , atp synthase , nitric oxide , biochemistry , microbiology and biotechnology , chemistry , neuronal nitric oxide synthase , biology , enzyme , biophysics , neuroscience , endocrinology
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, K m 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.