Abstract
Insulin, pancreatic polypeptide, glucagon, oxyntomodulin, and two distinct glucagon-like peptides were isolated from acidic ethanol extracts of bullfrog pancreas by gel filtration followed by high pressure liquid chromatography. The amino acid sequences of pancreatic polypeptide, oxyntomodulin, and both glucagon-like peptides were determined. Frog pancreatic polypeptide contains 36 amino acid residues and has a COOH-terminal phenylalaninamide. It is more homologous with human pancreatic polypeptide (61%) than other characterized members of this family of peptides. Frog glucagon has an amino acid composition identical to the NH2-terminal 29 residues of the larger, more abundant oxyntomodulin and was not sequenced. The finding of a single form of glucagon and oxyntomodulin, but two glucagon-like peptides in frog pancreas extract is similar to that found or deduced for mammals.
Highlights
From the Department of Biochemistry, University of Kansas Medical Center, Kansas City, Kansas 66103 and the $Veterans Administration Hospital, Kansas City, Missouri 64128
Frog glucagon has an amino acid radioimmunoassays, substances recognized by antisera specomposition identical to the NHz-termina2l9 residues cific for insulin, glucagon, somatostatin, and PP were found of the larger, more abundant oxyntomodulin andwas in extracts of the bullfrog pancreas [11]
Immunoassays tides which contain the amino acid sequences of the stored Insulin-like immunoreactivity in extracts and subsequent eluates and secreted forms of these peptide hormones, extracts of was assayed by a double antibody procedure using rabbit anti-porcine tissues may contain more than one active form of a hormone due to alternative RNA processing or differential post-translational processing
Summary
The evolution of the endocrine pancreas andthe types and numbers of endocrine cells found in islets and the identities and chemistry of their secreted hormonal peptides have been the subject of many studies [1,2,3]. PP are more recently discovered biologically active peptides variable wavelength detector. Immunoassays tides which contain the amino acid sequences of the stored Insulin-like immunoreactivity in extracts and subsequent eluates and secreted forms of these peptide hormones, extracts of was assayed by a double antibody procedure using rabbit anti-porcine tissues may contain more than one active form of a hormone due to alternative RNA processing or differential post-translational processing. Tracer ‘261-insulin was purchased from Du Pont-New England Nuclear. The tracer used was an HPLC-purified monoiodinated derivative of bovine PP prepared by reaction with monoiodinated ‘261-labeledBolton-Hunter reagent (Du Pont-New England Nuclear). High pressure liquid chromatography; GLP, glucagon-like peptide; Bullfrogs (R. catesbeiana) of both sexes and variable sizewere. GLP-I, thefirst glucagon-like peptide following glucagon in prepro- collected from local waters and kept a t 4 “Cuntil killed.
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