Purified guanylate cyclase: characterization, iodination and preparation of monoclonal antibodies.
Publication/Presentation Date
1-1-1980
Abstract
Guanylate cyclase was purified from the soluble fraction of rat lung using a modification of procedures published previously. The purified enzyme exhibited specific activities, at pH 7.6, of 219-438 nmoles/mg protein/min and 34-60 nmoles/mg protein/min with Mn2+ and Mg2+ as cation cofactors, respectively. The specific activity changed as a function of the protein concentration due to a change in Vmax with no alteration of the Km for GTP. The enzyme migrated as a single band coincident wih guanylate cyclase activity on nondenaturing polyacrylamide and isoelectric focusing gels (isoelectric point = 5.9). Purified guanylate cyclase had an apparent molecular weight of 150,000 daltons as determined by gel filtration chromatography and polyacrylamide gel electrophoresis. Electrophoresis in the presence of sodium dodecyl sulfate revealed a single subunit of 72,000 daltons, suggesting that the enzyme is a dimer of an identical subunit. The purified enzyme could be activated by nitric oxide, indicating that this compound interacts directly with the enzyme.
Volume
6
Issue
4
First Page
283
Last Page
296
ISSN
0095-1544
Published In/Presented At
Lewicki, J. A., Brandwein, H. J., Waldman, S. A., & Murad, F. (1980). Purified guanylate cyclase: characterization, iodination and preparation of monoclonal antibodies. Journal of cyclic nucleotide research, 6(4), 283–296.
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
6110682
Department(s)
Administration and Leadership
Document Type
Article