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Titlebook: Biochemistry, Molecular Biology, and Physiology of Phospholipase A2 and Its Regulatory Factors; Anil B. Mukherjee Book 1990 The Editor(s)

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https://doi.org/10.1007/978-3-663-08665-9als (4–9). More recently, we detected UG in the circulation of the rabbit (10). The source of this protein in circulation seems to be the tracheobronchial epithelium and/or the progesterone-induced uterine endometrium (10).
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Digitalisierung und Patientensicherheitstructure and enzymology of PLA., based on the paradigm of the pancreatic and snake venom enzymes, much remains to be learned regarding different cellular forms of PLA., their physiological roles, and how PLA. activity is regulated in cells.
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Probing the Mechanism of Pancreatic Phospholipase A2 with the Aid of Recombinant DNA Techniques,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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Inhibition of Phospholipase A2 by Uteroglobin and Antiflammin Peptides,als (4–9). More recently, we detected UG in the circulation of the rabbit (10). The source of this protein in circulation seems to be the tracheobronchial epithelium and/or the progesterone-induced uterine endometrium (10).
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Wulf-Dietrich Leber,Charlotte Vogt membrane bound and as cytosolic enzymes (2). Whereas the former acts intracellularly, the latter has the potential to be released from the cell upon a variety of stimuli (3). In humans, such soluble extracellular enzyme of pancreatic origin has indeed been found in the blood (4).
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MedR Schriftenreihe Medizinrechtes that hydrolyze the four ester bonds found in phospholipids. These enzymes are the phospholipases A., A., C, and D (2). Phospholipases A. and A. are responsible for cleaving the fatty acid ester bonds while phospholipases C and D cleave at the headgroup phosphoester bonds.
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