1978
DOI: 10.1016/0005-2744(78)90053-0
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Characterization of Guanylate cyclase of rod outer segments of the bovine retina

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Cited by 65 publications
(33 citation statements)
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“…The 308 IONIC MO VEMENTS IN RODS efficacy sequence for divalent cations in a nominally Na+-Ca2+-Mg2+-free solution containing 0-5 mM-IBMX, is: Mn2+ > Ba2+> (Ca2+, Co2+, Mg2+, Sr2+). This sequence is the same as the activation sequence for guanylate cyclase in vertebrate rods (Krishnan, Fletcher, Chader & Krishna, 1978) suggesting a possible dependence of selectivity also on guanosine-3' : 5'-cyclic monophosphate metabolism.…”
Section: The Selectivity Of the Light-sensitive Channelmentioning
confidence: 63%
“…The 308 IONIC MO VEMENTS IN RODS efficacy sequence for divalent cations in a nominally Na+-Ca2+-Mg2+-free solution containing 0-5 mM-IBMX, is: Mn2+ > Ba2+> (Ca2+, Co2+, Mg2+, Sr2+). This sequence is the same as the activation sequence for guanylate cyclase in vertebrate rods (Krishnan, Fletcher, Chader & Krishna, 1978) suggesting a possible dependence of selectivity also on guanosine-3' : 5'-cyclic monophosphate metabolism.…”
Section: The Selectivity Of the Light-sensitive Channelmentioning
confidence: 63%
“…But in the experiments supporting this view the solution changes were not fast enough to separate possible external and internal effects of divalent cations. For instance in rods treated with 0 5 mM-IBMX, Mn2+ appeared the most permeant cation, but since Mn2+ is known to be a potent activator of the cyclase (Krishnan, Fletcher, Chader & Krishna, 1978) it was difficult to separate direct effects on the channel from metabolic effects on cytoplasmic proteins. In the experiments shown in Figs 1 and 2 the slow activation of the photocurrent can be ascribed to the development of the IBMX effects or to more complex events in which the entry of divalent cations is affecting the cyclase or the phosphodiesterase.…”
Section: Resultsmentioning
confidence: 99%
“…Unlike the other particulate guanylate cyclase, rod outer segment guanylate cyclase is not solubilized by detergent treatment and is not activated by sodium azide (31,46) . In this study, 1 mM sodium azide had no effect on the reaction products, which is in agreement with the biochemical evidence.…”
Section: Discussionmentioning
confidence: 99%
“…Light or dark or some other accompanying factor, for example a calcium ion or other divalent metal ion (21), may affect the regulating site of guanylate cyclase. It is also possible that ion mobilization or ATP concentration may affect the guanylate cyclase activity (31).…”
Section: Discussionmentioning
confidence: 99%