The Amino Acid Sequence of Glucagon

Bromer, William W.; Sinn, L. G.; Staub, Alfred; Behrens, Otto K.

doi:10.2337/diab.6.3.234

Cited by 71 publications

(37 citation statements)

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“…This is not surprising since it is unlikely that the porcine glucagon differs in composition from ovine glucagon. Sequencing studies indicate that mammalian glucagons may be identical (Bromer et al 1971;Sundby and Markussen 1971).…”

Section: Discussionmentioning

confidence: 99%

Rates of Removal of Exogenous and Endogenous Glucagon From the Plasma of Sheep in Vivo

Brockman¹

1980

Aust. Jnl. Of Bio. Sci.

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The removal of exogenous and endogenous glucagon from plasma was determined in vivo in sheep weighing 53±1 (mean±s.e.) kg. Porcine glucagon was infused intravenously for 90 min. The metabolic clearance rates (MCR) were determined from plateau immunoreactive glucagon (IRG) concentrations in plasma and infusion rates of glucagon. The mean clearance rate (±s.e.) was 16·7±1·6 litres per hour (n = 20). Upon termination of the infusion, the decrease in IRG concentrations in plasma was determined. Least-squares regression analysis of non-linear functions indicated the data fit a two-component exponential function. The time constant for the rapid component of the plasma IRG disappearance function was -0·32±0·04 min-1 (mean±s.e.). The time constant for the slow component was -0·022±0·008 min-'. The rate of removal of endogenous glucagon was estimated during the infusion of somatostatin when glucagon secretion was inhibited. The time constants (mean±s.e., n = 8) for the decrease in IRG during somatostatin infusion were -0·42±0·08 and -0·003±0·002 min-' for fast and slow components, respectively. The time constants for the rapid components of exogenous and endogenous glucagon were not significantly different. This suggests that endogenous and exogenous glucagon are similarly removed from plasma.

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Section: Discussionmentioning

confidence: 99%

Rates of Removal of Exogenous and Endogenous Glucagon From the Plasma of Sheep in Vivo

Brockman¹

1980

Aust. Jnl. Of Bio. Sci.

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“…Glucagon is a 29-amino acid peptide (Bromer et al, 1956) originally isolated from a side fraction of purified insulin (Kenny, 1955) as a hyperglycemic factor originating from the pancreas (Kimball and Murlin, 1923). Its primary structure is identical in most mammals including man, although some amino acid sequence changes are noted in glucagons from guinea pig or nonmammalian vertebrates (Irwin, 2001).…”

Section: The Glucagon Receptormentioning

confidence: 99%

International Union of Pharmacology. XXXV. The Glucagon Receptor Family

et al. 2003

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“…A comparison of the amino acid sequence of the octacosapeptide with the sequences of the nonacosapeptide glucagon [26] and the heptacosapeptide secretin [22] all of porcine origin, shows ( Table 1) that starting with their N-terminal histidine residues the amino acid residues in positions 1, 2, 6 and 7 are identical in all three polypeptides, that residues 3, 12, 13, 14 and 23 of the octacosapeptide are identical to those of secretin but not of glucagon, and that conversely, its residues 10 and 28 are identical to those of glucagon but not of secretin. Since the octacosapeptide has a secretin-like action on the exorcine pancreas, and a glucagon-like action on the concentration of blood sugar [I], whereas secretin and glucagon, despite their extensive similarity in structure, do not exhibit each others' activities in these respects, although they do have similar actions on several other organs [27], it is not improbable that one or more of the 5 residues which are identical in the octacosapeptide and secretin, but not in glucagon, are necessary for the secretin-like activity of the octacosapeptide, and, probably, also for the activity of secretin itself.…”

Section: Hs D G T F T S E L S R Lmentioning

confidence: 99%

Structure of the Porcine Vasoactive Intestinal Octacosapeptide

Mutt

Said

1974

European Journal of Biochemistry

386

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The amino acid sequence of the porcine vasoactive intestinal octacosapeptide is His-Ser-AspAla-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-~ln-Met -Ala -Val -Lys -Lys -Tyr -Leu -AsnSer-Ile-Leu-Asn-NH,. Its amino acid residues 1, 2, 6 and 7, counted from the N-terminus, are identical to those in the corresponding positions in both porcine glucagon and secretin. The residues in positions 3, 12, 13, 14 and 23 are identical to those in secretin, but not in glucagon, and position 10 is occupied by a tyrosyl and position 28 by an asparaginyl residue, like in glucagon but not in secretin. If in addition to identical amino acid residues also chemically similar residues, such as isoleucine in position 26 of the octacosapeptide, as compared to leucine in secretin and glucagon, are taken into consideration then the similarity between these three polypeptides is still more evident.At a more remote level there is some structural resemblance also between these peptides and the other four peptides from the intestinal wall, cholecystokinin-pancreozymin, motilin, the gastric inhibitory peptide and substance P, the structures of which are known.The elucidation of the structure of the octacosapeptide was facilitated by the finding that pancreatic kallikrein preferentially cleaved only one of the three bonds in its N-terminal cyanogen bromide heptadecapeptide that are susceptible to cleavage with trypsin.In a previous paper [l] we reported that the porcine vasoactive intestinal octacosapeptide, like secretin and like glucagon, has an N-terminal histidylseryl structure. The complete amino acid sequence of the polypeptide has now been elucidated. Partial sequences have already been reported in publications on its synthesis [2,3] and the complete sequence too has recently been disclosed in a preliminary communication by Bodanszky et al. on the completion of the synthesis [4]. The present paper gives the evidence for the proposed sequence. MATERIALS AND METHODSPorcine vasoactive intestinal octacosapeptide was prepared as described earlier [l].Pancreatic kallikrein (sialidase -treated pig pancreatic kallikrein R, batch H 376) was a gift from Professor E. Werle, Munich. Tosyl-lysyl-chloromethyl ketone-treated chymotrypsin, proteinase K and L -(1 -tosylamido -2 -pheny1)ethyl chloromethylketone-treated trypsin, and carboxypeptidase A treated with diisopropyl phosphofluoridate from Worthington.L-Aspartic acid diamide -HCl, hemihydrate, was obtained from Cyclo Chemical, isoleucylleucine and leucylisoleucine from Fox Chemical Company and cyanogen bromide from Eastman Kodak.L-Asparagine-tert-butyl ester-HC1, L-aspartic aciddi-tert-butyl ester-HC1, tert-butyloxycarbonyl-L-asparagine p-nitrophenyl ester, and tert-butyloxycarbonyl-L-aspartic acid-p-tert-butyl-a-p-nitrophenyl ester were obtained from either Fox Chemical Company or from Bachem (Liestal, Switzerland).The sources and qualities of the other materials used have been described previously, as have the methods for paper chromatography and paper electrophoresis of peptides and for their h...

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The Amino Acid Sequence of Glucagon

Cited by 71 publications

References 0 publications

Rates of Removal of Exogenous and Endogenous Glucagon From the Plasma of Sheep in Vivo

Rates of Removal of Exogenous and Endogenous Glucagon From the Plasma of Sheep in Vivo

International Union of Pharmacology. XXXV. The Glucagon Receptor Family

Structure of the Porcine Vasoactive Intestinal Octacosapeptide

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