| pubmed-article:6307278 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6307278 | lifeskim:mentions | umls-concept:C1882810 | lld:lifeskim |
| pubmed-article:6307278 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:6307278 | lifeskim:mentions | umls-concept:C1413553 | lld:lifeskim |
| pubmed-article:6307278 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:6307278 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:6307278 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:6307278 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6307278 | pubmed:dateCreated | 1983-8-17 | lld:pubmed |
| pubmed-article:6307278 | pubmed:abstractText | The calmodulin-dependent cyclic AMP phosphodiesterase and cyclic GMP phosphodiesterase (EC 3.1.4.17) activity of rat pancreas was purified 280-fold by affinity chromatography on calmodulin-Sepharose 4B. It then accounted for 15% of the total cytosol cyclic GMP nucleotide phosphodiesterase activity, in the presence of Ca2+, and represented a minor component of proteins specifically adsorbed by the column. This activity was resolved on a DEAE-Sephacel column into two fractions, termed PI and PII, on the basis of their order of emergence. After this step, PI and PII were purified 5650- and 3700-fold respectively. The molecular weight of PI was 175 000 and that of PII was 116 000, by polyacrylamide-gradient-gel electrophoresis. Both forms of phosphodiesterase could hydrolyse cyclic AMP and cyclic GMP, although PII displayed a higher affinity toward cyclic GMP than toward cyclic AMP. PI and PII exhibited negative homotropic kinetics in the absence of calmodulin. Upon addition of calmodulin, both enzymes displayed Michaelis-Menten kinetics and a 5-9-fold increase in maximal velocity, at physiological concentrations of cyclic GMP and cyclic AMP. When a pancreatic extract freshly purified by affinity chromatography was immediately analysed by high-performance gel-permeation chromatography on a TSK gel G3000 SW column, PII represented as much as 78% of the eluted activity. This percentage decreased to 52% when the sample was stored at 0 degrees C for 20 h before analysis, suggesting that PII, possibly predominant in vivo, was converted into the heavier PI form upon storage. | lld:pubmed |
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| pubmed-article:6307278 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6307278 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6307278 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6307278 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6307278 | pubmed:month | May | lld:pubmed |
| pubmed-article:6307278 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6307278 | pubmed:author | pubmed-author:ChristopheJJ | lld:pubmed |
| pubmed-article:6307278 | pubmed:author | pubmed-author:VandermeersAA | lld:pubmed |
| pubmed-article:6307278 | pubmed:author | pubmed-author:Vandermeers-P... | lld:pubmed |
| pubmed-article:6307278 | pubmed:author | pubmed-author:RatheJJ | lld:pubmed |
| pubmed-article:6307278 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6307278 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:6307278 | pubmed:volume | 211 | lld:pubmed |
| pubmed-article:6307278 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6307278 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6307278 | pubmed:pagination | 341-7 | lld:pubmed |
| pubmed-article:6307278 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:6307278 | pubmed:meshHeading | pubmed-meshheading:6307278-... | lld:pubmed |
| pubmed-article:6307278 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6307278 | pubmed:articleTitle | Purification and kinetic properties of two soluble forms of calmodulin-dependent cyclic nucleotide phosphodiesterase from rat pancreas. | lld:pubmed |
| pubmed-article:6307278 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6307278 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:6307278 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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