Activity stain for the detection of cyclic nucleotide phosphodiesterase separated by polyacrylamide gel electrophoresis and its application to the cyclic nucleotide phosphodiesterase of beef heart
✍ Scribed by Elihu N. Goren; Allen H. Hirsch; Ora M. Rosen
- Publisher
- Elsevier Science
- Year
- 1971
- Tongue
- English
- Weight
- 604 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
Cyclic 3',5'-nucleotide phosphodiesterase, which was originally purified from beef heart (1)) has since been reported to occur in the soluble fraction from a variety of tissues (2-5). In view of the widespread interest in the role of these phosphodiesterases in cyclic nucleotide metabolism, and the frequent use of polyacrylamide gel electrophoresis for the detection and purification of enzymes, the development of a method for localizing the activity of this enzyme in gel matrices was considered desirable. This report describes a simple method for the rapid localization of cyclic nucleotide phosphodiesterase activity in acrylamide gels based upon the methods used for the detection of alkaline phosphatase (6,7). A similar method has been used by Shanta et al. ( 8) for the histochemical localization of cyclic nucleotide phosphodiesterase. Using this method, two electrophoretically distinct bands of cyclic nucleotide phosphodiesterase activity have been detected in preparations derived from beef heart.