Abstract
A combination of three HPLC procedures applied to the venom of Gila monster (Heloderma suspectum) has led to the purification to homogeneity of two bioactive components: (i) a 17.5 kDa protein, isolated on the basis of its potent secretory effect on dispersed rat pancreatic acini, was accordingly designated PSF (pancreatic secretory factor); (ii) a 5.9-kDa peptide, designated helodermin, was purified on the basis of its ability to stimulate adenylate cyclase in rat pancreatic membranes. PSF was unable to activate adenylate cyclase and, conversely, helodermin was devoid of secretory action.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adenylyl Cyclases / metabolism
-
Animals
-
Biological Assay
-
Cell Membrane / enzymology
-
Chromatography, High Pressure Liquid / methods
-
Enzyme Activation
-
Intercellular Signaling Peptides and Proteins
-
Lizards*
-
Molecular Weight
-
Pancreas / enzymology
-
Pancreatic Juice / drug effects
-
Pancreatic Juice / metabolism
-
Peptides / isolation & purification*
-
Peptides / pharmacology
-
Rats
-
Secretin
-
Vasoactive Intestinal Peptide
-
Venoms / analysis*
Substances
-
Intercellular Signaling Peptides and Proteins
-
Peptides
-
Venoms
-
pancreatic secretory factor, Gila monster venom
-
Secretin
-
Vasoactive Intestinal Peptide
-
heliodermin
-
Adenylyl Cyclases