A Two-Step Procedure for Obtaining Highly Purified Particulate Guanylate Cyclase From Rat Lung

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Abstract
Guanylate cyclase (GTP pyrophosphate lyase (cyclizing), EC 4.6.1.2), the enzyme catalyzing the formation of cyclic GMP, from GTP, exists in both soluble and membrane-bound forms. These enzymes have been implicated as key regulatory components in a variety of biological events such as secretion and smooth muscle relaxation. Understanding the role these enzymes play in cellular regulation is predicted upon obtaining purified preparations of guanylate cyclase. Several procedures for purifying the soluble enzyme to apparent homogeneity from a variety of tissues have been reported. The particulate enzyme has been purified to apparent homogeneity from sea urchin sperm but, to date, homogeneous preparations of particulate guanylate cyclase from mammalian tissues have not been obtained. Here we report our efforts in purifying particulate guanylate cyclase about 8,200- to 52,000-fold from homogeneous of rat lung. Portions of this work have appeared in abstract form.