Cyclic AMP phosphodiesterases of Funaria hygrometrica

Sharma, Shobhona ; Johri, Man Mohan (1983) Cyclic AMP phosphodiesterases of Funaria hygrometrica Phytochemistry, 22 (12). pp. 2715-2717. ISSN 0031-9422

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High affinity cAMP phosphodiesterase (PDE) activity has been purified (ca 474-fold) from the chloronema cells of the moss Funaria hygrometrica. The activity in the 15 000 g supernatant was precipitated at 40-80% saturation with (NH4)2SO4 and separated by DEAE-cellulose chromatography into two peaks of activity A and B with pH optima at pH 5.5 and 7.5, respectively. When rechromatographed on DEAE-cellulose, the PDE B activity redistributed into two peaks (A'and B'). The recovery of PDE activity in the latter peaks suggests a conversion of alkaline PDE into acid PDE. The phosphodiesterase activity B was further resolved by affinity chromatography on a cAMP-agarose column into PDE I and PDE II. The latter was free from nucleotidases, was Ca2+-dependent and showed only a high-affinity component towards cAMP as the substrate, the Km being 11.8 ± 4.8 µ M.

Item Type:Article
Source:Copyright of this article belongs to Phytochemical Society of Europe.
Keywords:Funaria hygrometrica; Bryidae; Moss; Protonema; Cyclic AMP Phosphodiesterase; High-affinity; Calcium Dependence
ID Code:14968
Deposited On:13 Nov 2010 13:13
Last Modified:23 Feb 2011 11:33

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