PURIFIED RETINAL NITRIC-OXIDE SYNTHASE ENHANCES ADP-RIBOSYLATION OF ROD OUTER SEGMENT PROTEINS

Authors
Citation
M. Zoche et Kw. Koch, PURIFIED RETINAL NITRIC-OXIDE SYNTHASE ENHANCES ADP-RIBOSYLATION OF ROD OUTER SEGMENT PROTEINS, FEBS letters, 357(2), 1995, pp. 178-182
Citations number
37
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
357
Issue
2
Year of publication
1995
Pages
178 - 182
Database
ISI
SICI code
0014-5793(1995)357:2<178:PRNSEA>2.0.ZU;2-S
Abstract
Nitric oxide synthase is present in different cell layers of vertebrat e retina and seems to have neuromodulatory functions in the outer reti na, The enzyme, when purified from a bovine retina extract, has an app arent molecular mass of 160 kDa and resembles the neuronal constitutiv e NOS type I with respect to Ca2+-calmodulin sensitivity, K-m value an d inhibition by analogues of L-arginine. Retinal NOS is present in a p reparation of rod outer segments attached to parts of the inner segmen ts, but not in pure outer segments. We describe the enhancement of spe cific ADP-ribosylation of outer segment proteins by purified retinal N OS.