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Guanylate cyclase from bovine lung. A kinetic analysis of the regulation of the purified soluble enzyme by protoporphyrin IX, heme, and nitrosyl-heme.

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Wolin, M S, Wood, K S, Ignarro, L J·1982·Journal of Biological Chemistry

Abstract

A kinetic characterization of the regulation of purified soluble guanylate cyclase from bovine lung by protoporphyrin M and hematin is reported.Purified guanylate cyclase was isolated with heme and had specific activities @mol of cGMP/min/mg of protein) of 0.1-0.2 and 0.3-0.6 in the presence of excess MgGTP and MnGTP, respectively, in the absence of added activators.Protoporphyrin IX, nitric oxide (NO), and NOheme increased the V,, up to 40-fold and decreased the K,,, for GTP (from 100 to 45-55 p ~) in the presence of excess Mg'.However, in the presence of excess Mn2+ the V,, was increased only slightly and the K , for GTP was unchanged.Protoporphyrin IX resembled NO and NO-heme also in lowering the K , and Ki for uncomplexed metal.This close similarity in the interactions of these activators with guanylate cyclase suggests that a common form of activated enzyme is generated.Hematin, in excess of 1.5 p ~, inhibited guanylate cyclase activity.Smaller concentrations of hematin competitively inhibited protoporphyrin IX (KI = 0.35 p ~) ,

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Metadata

Authors
Wolin, M. S., Wood, K. S., & Ignarro, L. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1982-11
Volume
257
Issue
22
Pages
13312-13320
ISSN
0021-9258 (ISSN-L)
OpenAlex
W105256667
Cited by
185
References
1
FWCI
2.28
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Guanylate cyclase from bovine lung. A kinetic analysis of the regulation of the purified soluble enzyme by protoporphyrin IX, heme, and nitrosyl-heme. https://app.cochat.ai/papers/10.1016/s0021-9258(18)33448-3
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Wolin, M. S., Wood, K. S., & Ignarro, L. J. (1982). Guanylate cyclase from bovine lung. A kinetic analysis of the regulation of the purified soluble enzyme by protoporphyrin IX, heme, and nitrosyl-heme. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)33448-3

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