Premium
High levels of pancreatic nonspecific lipase in rattlesnake and leopard shark
Author(s) -
Patton John S.
Publication year - 1975
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02532361
Subject(s) - lipase , monoglyceride , monoacylglycerol lipase , glycerol , chemistry , hydrolysis , stearate , glyceride , fatty acid , triacylglycerol lipase , biochemistry , oleic acid , food science , enzyme , biology , endocannabinoid system , organic chemistry , receptor
Abstract Hydrolysis of synthetic triglycerides by rattlesnake and leopard shark pancreatic enzymes revealed striking differences in specificity, depending on the presence or absence of sodium taurocholate. Without added sodium taurocholate the classical specificity of pancreatic lipase was expressed. Rattlesnake enzymes, in the presence of sodium taurocholate, attacked the unsaturated oleic acid in the 2‐position of racemic glycerol‐1‐palmitate‐2‐oleate‐3‐stearate nearly twice as fast as either outside saturated fatty acid. In this instance, over 90% of the monoglyceride which accumulated were 1‐monoglyceride. These results are attributed to very high levels of bile salt activated nonspecific lipase. Eight vertebrate species were compared. With the exception of the rattlesnake and leopard shark, the other species (3 elasmobranchs and 3 mammals) all exhibited low levels of non‐specific lipase, e.g. less than 5% hydrolysis of the 2‐position of racemic glycerol‐1‐palmitate‐2‐oleate‐3‐stearate in the presence of sodium taurocholate.