Isolation of a Glucagon-containing Peptide: Primary Structure of a Possible Fragment of Proglucagon
AUTOR(ES)
Tager, Howard S.
RESUMO
The heterogeneity of crystalline bovine (ox)/porcine glucagon has been examined by gel filtration and ion-exchange chromatography. A strongly basic peptide that reacted well with antibodies to bovine/porcine glucagon was isolated and its primary structure was determined. The amino-acid sequence of the NH2-terminal 29 residues of the 4500-dalton peptide is identical with that of intact bovine or porcine glucagon. The remaining eight residues at its COOH-terminus are Lys-Arg-Asn-Asn-Lys-Asn-Ile-Ala. Small amounts of other glucagon-immunoreactive peptides having molecular weights ranging from 3700 to 9000 were also detected in crystals of bovine/porcine glucagon. We propose that the 37-residue peptide is a fragment of bovine or porcine proglucagon.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433727Documentos Relacionados
- Histidyl-proline diketopiperazine (His-Pro DKP) immunoreactivity is present in the glucagon-containing cells of the human fetal pancreas.
- Conversion of proglucagon in pancreatic alpha cells: the major endproducts are glucagon and a single peptide, the major proglucagon fragment, that contains two glucagon-like sequences.
- Crystal structure of the major histocompatibility complex class I H-2Kb molecule containing a single viral peptide: implications for peptide binding and T-cell receptor recognition.
- Crystal structure of [Leu1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms.
- Induction of intracellular cAMP by a synthetic retroviral envelope peptide: a possible mechanism of immunopathogenesis in retroviral infections.