High levels of pancreatic nonspecific lipase in rattlesnake and leopard shark.
Lipids
confidence
Key findings
Rattlesnake and leopard shark pancreas show high bile-salt-activated nonspecific lipase; in vitro biochemical specificity study, no clinical endpoints.
View source on PubMed (PMID 1177670) ↗
- Sample size
- 8 species
- Population
- Eight vertebrate species (rattlesnake, leopard shark, 3 elasmobranchs, 3 mammals)
- Route
- in vitro enzymatic assay
- Blinding
- not_reported
- Controls
- none
- Drug class
- digestive enzyme blend
Full 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 nonspecific 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.