Abstract:
:Receptor-mediated regulation of guanylate cyclase is well-studied in intact Dictyostelium discoideum cells, but study of the enzyme in cell-free preparations has hampered. A major obstacle has been that in vitro guanylate cyclase activity could be detected only in the presence of unphysiological concentrations of Mn2+-ions. In this paper we report the identification of a guanylate cyclase in D.discoideum cell homogenates that has high activity with Mg2+-GTP. The enzyme is activated by non-hydrolyzable ATP and GTP analogues and inhibited by submicromolar concentrations of Ca2+-ions. We suggest that the presently identified enzyme is regulated in intact cells via cell surface receptors. The compounds that modulated the enzyme activity in vitro may reflect physiologically relevant regulation mechanisms.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Janssens PM,de Jong CCdoi
10.1016/0006-291x(88)90535-9subject
Has Abstractpub_date
1988-01-15 00:00:00pages
405-11issue
1eissn
0006-291Xissn
1090-2104pii
0006-291X(88)90535-9journal_volume
150pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
pub_type: 杂志文章
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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