Abstract
Phospholipase A2 (E.C. 3.1.1.4) attacks the acyl ester bond at position 2 of 3-sn-phosphoglycerides (van Deenen en de Haas, 1963). The in-vivo importance of phospholipase A2 (PLA) is reflected by the fact that this enzyme occurs ubiquitously in nature and that PLA activity has been detected in a large number of cell types and cell organelles. In general their physiological role can be either a digestive or a regulatory one. The extracellular PLAS from mammalian pancreas and snake venom, which are responsible for the hydrolysis of dietary phospholipid, predominantly belong to the first class of PLAs, the digestive enzymes. To the cellular PLAs have been assigned regulatory functions (for a review see Waite, 1987), although certain cellular PLAs also exhibit a digestive role in the break-down of phagocytized materials (Elsbach and Weiss, 1988).
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Kuipers, O.P., van den Bergh, C.J., Verheij, H.M., de Haas, G.H. (1990). Probing the Mechanism of Pancreatic Phospholipase A2 with the Aid of Recombinant DNA Techniques. In: Mukherjee, A.B. (eds) Biochemistry, Molecular Biology, and Physiology of Phospholipase A2 and Its Regulatory Factors. Advances in Experimental Medicine and Biology, vol 279. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0651-1_5
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DOI: https://doi.org/10.1007/978-1-4613-0651-1_5
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