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Cationic factors affecting phospholipase activities from human lung
| Content Provider | Scilit |
|---|---|
| Author | Yeats, D. A. Bakhle, Y. S. |
| Copyright Year | 1990 |
| Description | Journal: British Journal of Pharmacology 1 The effects of varying $H^{+}$ and other cation concentrations on phospholipase activity were investigated on two particulate fractions from human lung, corresponding to the mitochondrial and microsomal fractions. 2 Three$ ^{14}$C-labelled substrates, arachidonyl-phosphatidylcholine (PC), -phosphatidylethanolamine (PE) and -phosphatidylinositol (PI) were used. 3 For two substrates, PE and PI, hydrolysis was maximal at pH 6, with either subcellular fraction. 4 Hydrolysis of all three substrates was strongly inhibited by EDTA and EGTA (10–25 mm). Addition of 2,2-dipyridyl, o-phenanthroline, 8-hydroxyquinoline or desferrioxamine (10 μm-1 mm) did not inhibit but often increased hydrolysis of all substrates. 5 Addition of $Zn^{2+}$, as $ZnCl_{2}$, (10 μm-1 mm) inhibited PE and PI, but not PC, hydrolysis. 6 The phospholipase activities from human lung appear to be dependent on $Ca^{2+}$ for maximal activity and to be inhibited by other metal ions including $Zn^{2+}$. |
| Related Links | http://europepmc.org/articles/pmc1917788?pdf=render https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1476-5381.1990.tb15826.x |
| Ending Page | 452 |
| Page Count | 6 |
| Starting Page | 447 |
| e-ISSN | 14765381 |
| DOI | 10.1111/j.1476-5381.1990.tb15826.x |
| Journal | British Journal of Pharmacology |
| Issue Number | 3 |
| Volume Number | 100 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 1990-07-19 |
| Access Restriction | Open |
| Subject Keyword | Journal: British Journal of Pharmacology Phospholipase Activities Human Lung |
| Content Type | Text |
| Resource Type | Article |
