| Literature DB >> 9056231 |
R K Sharma1, Y Tan, R V Raju.
Abstract
Calmodulin-dependent cyclic nucleotide phosphodiesterase was identified in and purified to apparent homogeneity from the total calmodulin-binding protein fraction of bovine eye in a single step by immunoaffinity chromatography. The bovine eye calmodulin-dependent cyclic nucleotide phosphodiesterase is immunologically similar to the bovine brain 60-kDa isozyme. The purified enzyme had higher affinity for calmodulin than the 60-kDa phosphodiesterase isozyme from bovine brain, but similar affinity to that of the heart isozyme. When the Ca(2+)-dependence of the eye enzyme was compared to cardiac calmodulin-dependent cyclic nucleotide phosphodiesterase at an identical concentration of calmodulin, the bovine eye calmodulin-dependent cyclic nucleotide phosphodiesterase was activated at the same Ca2+ concentration as the bovine heart calmodulin-dependent cyclic nucleotide phosphodiesterase isozyme.Entities:
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Year: 1997 PMID: 9056231 DOI: 10.1006/abbi.1996.9837
Source DB: PubMed Journal: Arch Biochem Biophys ISSN: 0003-9861 Impact factor: 4.013