Cyclic nucleotide phosphodiesterase and 5′-nucleotidase: A coupled system
Neurochemical Research, ISSN: 1573-6903, Vol: 14, Issue: 12, Page: 1213-1221
1989
- 2Citations
- 1Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations2
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- CrossRef2
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Article Description
Evidence is presented that multiple forms of cyclic nucleotide phophodiesterase (PDE) activity chromatographically separated from the soluble fraction of bovine hypothalamus are co-eluted with multiple forms of 5′-nucleotidase (5′N) activity. The enzymes could not be resolved from each other by anion-exchange chromatography on DEAE-TSK; by affinity chromatography on phenyl-, blue-, concanavalin A-, 5′ AMP-sepharose, cAMP-silica gel; or by gel filtration on sephacryl S-200. The catalytic activities were found to be associated with the tetrameric, dimeric, and monomeric forms of the enzymes. The molecular weights determined by gel filtration or by SDS-gel electrophoresis were 220, 114, and 57 kDa, respectively. Kinetic analysis revealed that the first-order rate constant for 5′ AMP hydrolysis measured in the reactions: cAMP→5′AMP→adenosine was 100 times higher than that in the reaction: 5′AMP→adenosine. Thus, functional interrelation between PDE and 5′N was expressed in drastic acceleration of the consecutive reactions: cAMP →5′AMP→adenosine. The results confirm the conclusion about the existence of a multienzyme system involving PDE and 5′N or of a single bifunctional enzyme in brain tissue. © 1989 Plenum Publishing Corporation.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0024840193&origin=inward; http://dx.doi.org/10.1007/bf00965512; http://www.ncbi.nlm.nih.gov/pubmed/2560820; http://link.springer.com/10.1007/BF00965512; http://www.springerlink.com/index/pdf/10.1007/BF00965512; http://www.springerlink.com/index/10.1007/BF00965512; https://dx.doi.org/10.1007/bf00965512; https://link.springer.com/article/10.1007/BF00965512
Springer Nature
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