
The rat pancreas shows a phospholipase activity in the absence of the tryptic activation of the zymogens. We verified that this activity was not due to the zymogen of the secretory phospholipase. Indeed unlike the prophospholipase, the enzyme responsible for the spontaneous phospholipase activity shows a higher catalytic rate at substrate concentrations higher than the critical micelle concentration. This enzyme has a positional specificity of the A2 type and possesses a molecular weight of about 9,500.
Male, Phospholipases A2, Phospholipases, Phosphatidylethanolamines, Animals, Pancreas, Micelles, Phospholipases A, Rats, Substrate Specificity
Male, Phospholipases A2, Phospholipases, Phosphatidylethanolamines, Animals, Pancreas, Micelles, Phospholipases A, Rats, Substrate Specificity
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 7 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
