Purification and Sequence of Rat Oxyntomodulin (Enteroglucagon/Peptide/Intestine/Proglucagon/Radlolmmunoassay) NATHAN L
Proc. Nati. Acad. Sci. USA Vol. 91, pp. 9362-9366, September 1994 Biochemistry Purification and sequence of rat oxyntomodulin (enteroglucagon/peptide/intestine/proglucagon/radlolmmunoassay) NATHAN L. COLLIE*t, JOHN H. WALSHO, HELEN C. WONG*, JOHN E. SHIVELY§, MIKE T. DAVIS§, TERRY D. LEE§, AND JOSEPH R. REEVE, JR.t *Department of Physiology, School of Medicine, University of California, Los Angeles, CA 90024; *Center for Ulcer Research and Education, Gastroenteric Biology Center, Department of Medicine, Veterans Administration Wadsworth Center, School of Medicine, University of California, Los Angeles, CA 90073; and §Division of Immunology, Beckman Institute of City of Hope Research Institute, Duarte, CA 91010 Communicated by Jared M. Diamond, May 26, 1994 ABSTRACT Structural information about rat enteroglu- glucagon plus two glucagon-like sequences (GLP-1 and -2) cagon, intestinal peptides containing the pancreatic glucagon arranged in tandem. The present study concerns the enter- sequence, has been based previously on cDNA, immunologic, oglucagon portion of proglucagon (i.e., the N-terminal 69 and chromatographic data. Our interests in testing the phys- residues and its potential cleavage fragments). iological actions of synthetic enteroglucagon peptides in rats Our use of the term "enteroglucagon" refers to intestinal required that we identify precisely the forms present in vivo. peptides containing the pancreatic glucagon sequence. Fig. 1 From knowledge of the proglucagon gene sequence, we syn- shows two proposed enteroglucagon forms, proglucagon-(1- thesized an enteroglucagon C-terminal octapeptide common to 69) (glicentin) and proglucagon-(33-69) (OXN; see Fig. 1). both proposed enteroglucagon forms, glicentin and oxynto- The primary structures based on amino acid sequence data of modulin, but sharing no sequence overlap with glucagon.
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