Purification and characterization of guanylate cyclase from Caulobacter crescentus期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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Purification and characterization of guanylate cyclase from Caulobacter crescentus

Authors:	I C Sun L Shapiro O M Rosen

Institution:	1. Department of Molecular Biology, Division of Biological Sciences, Albert Einstein College of Medicine, Bronx, New York 10461 USA;2. The Department of Medicine, Albert Einstein College of Medicine, Bronx, New York 10461 USA

Abstract:	Guanylate cyclase has been purified 60-fold from cell extracts of the bacterium $Caulobacter crescentus$ . It has a molecular weight of approximately 140,000 and is dependent upon Mn²⁺ for activity. Enzymic activity is unaffected by cyclic AMP, cyclic GMP or N⁶,O^2′-dibutyryl cyclic AMP but is stimulated by N²,O^2′-dibutyryl cyclic GMP. The partially purified preparation of guanylate cyclase does not contain detectable adenylate cyclase activity.

Keywords:	Address all correspondence to: Irene C Sun Department of Molecular Biology Albert Einstein College of Medicine 1300 Morris Park Avenue Bronx New York 10461
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