Protoporphyrin IX activates the Mg dependent guanylate cyclase from rat liver plasma membranes.

Abstract:

:In the presence of Mg-GTP, the rat liver guanylate cyclase, in either intact membranes or trypsin solubilized form, was stimulated by protoporphyrin IX 6 to 10-fold. However, when Mn-GTP was the substrate, protoporphyrin IX activated the membrane-bound guanylate cyclase only 50%, in contrast to the marked activation reported for the cytosolic enzyme. Meso- and deuteroporphyrin IX, hematoporphyrin and coproporphyrin III also activated membrane guanylate cyclase while uroporphyrin III, and hemin had no effect. Basal, Mg2+-dependent activity exhibited two classes of catalytic sites with apparent Km values of 2 mM and 0.12 mM. Activation by protoporphyrin resulted in the disappearance of the low affinity sites. The activated enzyme exhibited Michaelis-Menten kinetics and no alteration in its requirement for excess Mg2+. These data indicate that, in the presence of Mg2+, a heme-like structure can interact with the membrane-bound guanylate cyclase and regulate its activity.

authors

Lacombe ML,Eberentz-Lhomme C

doi

10.1016/0006-291x(83)90378-9

subject

Has Abstract

pub_date

1983-10-14 00:00:00

pages

47-53

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(83)90378-9

journal_volume

116

pub_type

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