Purification and Properties of Periplasmic 3’:5’-Cyclic Nucleotide Phosphodiesterase
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چکیده
منابع مشابه
Purification and properties of the light-activated cyclic nucleotide phosphodiesterase of rod outer segments.
Frog (Rana catesbiana) rod outer segment disc membranes contain a cyclic nucleotide phosphodiesterase (EC 3.1.4.17) which is activated by light in the presence of ATP. This enzyme is firmly bound to the disc membrane, but can be eluted from the membrane with 10 mM Tris-HCl buffer, pH 7.4 and 2 mM EDTA. The eluted phosphodiesterase has reduced activity, but can be activated approximately 10-fold...
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Calmodulin-dependent cyclic nucleotide phosphodiesterase was purified from bovine brain to apparent homogeneity by a new procedure involving DEAE-cellulose, Affi-Gel blue, calmodulin-Sepharose 4B, and Sephadex G-200 column chromatographies. The enzyme was purified more than 3,000-fold from the brain extracts with greater than 12% yield. The purified phosphodiesterase could be activated 10- to 1...
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Cyclic nucleotides have been implicated in the differentiation and function of the vertebrate retina. In the normal retina of DBA mice, the specific activity of cyclic-nucleotide phosphodiesterase (PDE), with cyclic-AMP as the substrate (cAMP-PDE), increases eightfold between the 6th and 20th postnatal day. Kinetic analysis of retinae from newborn mice reveals a PDE with a single Michaelis cons...
متن کامل3'-cyclic nucleotide 3'-phosphodiesterase
1. A spectrophotometric assay of 2':3'-cyclic nucleotide 3'-phosphodiesterase (EC 3.1.4.37) based on the use of an acid-base indicator and a buffer having identical PKa values is described. The assay is sinmple and rapid; it was particularly convenient for monitoring the enzyme activity at vat :ous stages of purification. 2. Several proteinases were examined for their ability to solubilize 2':3...
متن کاملPurification to homogeneity and general properties of a novel phosphodiesterase hydrolyzing cyclic CMP and cyclic AMP.
A cytidine 3’5’-monophosphate (cyclic CMP) phosphodiesterase was purified more than 10,000-fold to apparent homogeneity from the pig liver extract by the steps of pH and ammonium sulfate fractionations, and DEAE-cellulose, Sephadex G-100, and 8-HzN(CH&NHcyclic AMP Sepharose 4B affinity chromatographies. The preparation appeared as a single protein band in sodium dodecyl sulfate-polyacrylamide g...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.29.17627