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THE PHOSPHOLIPASE ACTIVITY OF SHEEP PANCREATIC JUICE
Author(s) -
Arienti G.,
Leat W. M. F.,
Harrison F. A.
Publication year - 1975
Publication title -
quarterly journal of experimental physiology and cognate medical sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.925
H-Index - 101
eISSN - 1469-445X
pISSN - 0033-5541
DOI - 10.1113/expphysiol.1975.sp002286
Subject(s) - lysophospholipase , phospholipase , lecithin , pancreatic juice , hydrolysis , biochemistry , phospholipase a1 , chemistry , enzyme , phospholipase a2 , fatty acid , phospholipase a , lipase , biology , pancreas
Sheep pancreatic juice was found to contain at least two enzymes which hydrolysed biliary lecithin. One enzyme was heat and acid labile and hydrolysed the fatty acid from position 1 (phospholipase A 1 ); the other was heat and acid stable hydrolysing the fatty acid at position 2(phospholipase A 2 ). Lysophospholipase activity was also present. The phospholipases were active at pH values greater than 4·2, and would therefore function in the acid conditions (pH 3–6) of the sheep small intestine. The activity of the pancreatic phospholipases, and A 2 in particular, was dramatically stimulated by the presence of the secretions of Brunner's glands which could be important in accelerating the hydrolysis of biliary lecithin in the lumen of the intestine. Phospholipase A 1 was sensitive to acid in the range pH 2·5—3·5 and could therefore be partially inactivated by abomasal digesta; but phospholipase A 2 was resistent to acid treatment.