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- W4255157095 abstract "Two high molecular weight proteins with phospholipase activity (Phospholipase-I and Phospholipase-II) were found to be present in the homogenate of porcine pancreas without delipidation and heat treatments. Phospholipase-I had an isoelectric point (pI) of about 4.5, while Phospholipase-II about 6.0. Both the Phospholipase-I and -II were purified by isoele-ctric focusing and gel filtration on Sephadex G-200. The molecular weights of both enzymes are about 5×105. Two enzymes differed greatly from each other in the heat stability and the effect of pH on the activities. Phospholipase-I (pI 4.5) was converted to the fraction with pI 6.0 by extraction of lipids, while Phospholipase-II (pI 6.0) to the fraction with pI 4.5 by addition of the extracted lipids in a yield of about 50%. These converted enzymes were very similar to the corresponding native enzymes in the properties above described, respectively. These results suggest that the Phospholipase-I may exist as a Phospholipase-II-lipid complex. Furthermore, the relationship among the Phospholipase-I, Phospholipase-II, and the phospholipase A2 reported by de Haas et al. are discussed." @default.
- W4255157095 created "2022-05-12" @default.
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- W4255157095 date "1979-01-01" @default.
- W4255157095 modified "2023-09-26" @default.
- W4255157095 title "Occurrence of two high molecular phospholipases with different isoelectric points in porcine pancreas and their reversible interconversion." @default.
- W4255157095 doi "https://doi.org/10.1271/bbb1961.43.981" @default.
- W4255157095 hasPublicationYear "1979" @default.
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