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Titolo:
PURIFICATION AND SEQUENCE OF RAT OXYNTOMODULIN
Autore:
COLLIE NL; WALSH JH; WONG HC; SHIVELY JE; DAVIS MT; LEE TD; REEVE JR;
Indirizzi:
TEXAS TECH UNIV,DEPT BIOL SCI LUBBOCK TX 79409 UNIV CALIF LOS ANGELES,SCH MED,DEPT PHYSIOL LOS ANGELES CA 90024 UNIV CALIF LOS ANGELES,VET ADM WADSWORTH MED CTR,SCH MED,DEPT MED,CTRGASTROENTER BIOL LOS ANGELES CA 90073 CITY HOPE RES INST,BECKMAN INST,DIV IMMUNOL DUARTE CA 91010
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 20, volume: 91, anno: 1994,
pagine: 9362 - 9366
SICI:
0027-8424(1994)91:20<9362:PASORO>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCES; MICROSEQUENCE ANALYSIS; INTESTINAL ADAPTATION; GENE-EXPRESSION; PROGLUCAGON; PEPTIDES; GLICENTIN; GLUCAGON; PANCREAS; PROTEINS;
Keywords:
ENTEROGLUCAGON; PEPTIDE; INTESTINE; PROGLUCAGON; RADIOIMMUNOASSAY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
20
Recensione:
Indirizzi per estratti:
Citazione:
N.L. Collie et al., "PURIFICATION AND SEQUENCE OF RAT OXYNTOMODULIN", Proceedings of the National Academy of Sciences of the United Statesof America, 91(20), 1994, pp. 9362-9366

Abstract

Structural information about rat enteroglucagon, intestinal peptides containing the pancreatic glucagon sequence, has been based previouslyon cDNA, immunologic, and chromatographic data. Our interests in testing the physiological actions of synthetic enteroglucagon peptides in rats required that we identify precisely the forms present in vivo. From knowledge of the proglucagon gene sequence, we synthesized an enteroglucagon C-terminal octapeptide common to both proposed enteroglucagon forms, glicentin and oxyntomodulin, but sharing no sequence overlap with glucagon. We then developed a radioimmunoassay using antibodies raised against the octapeptide that was specific for enteroglucagon peptides without cross-reacting with glucagon. Rat intestine was extracted, and one presumptive enteroglucagon form was purified by following the enteroglucagon C-terminal octapeptide-like immunoreactivity throughseveral HPLC purification steps. Structural characterization of the material by amino acid composition, microsequence, and mass spectral analyses identified the peptide as rat oxyntomodulin. The 37-residue peptide consists of pancreatic glucagon plus the C terminal extension, Lys-Arg-Asn-Arg-Asn-Asn-Ile-Ala. This now permits synthesis of an unambiguous duplicate of endogenous rat oxyntomodulin for physiological studies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 03:13:16