Biological Activity and Clearance of Gastrin Peptides in Dog and Man: Effects of Varying Chain Length of Peptide Fragments

  • J. H. Walsh
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 106)


Gastrin is known to exist in mammalian tissues and blood in multiple molecular forms. Six of these forms have been characterized chemically and shown to be three pair of single chain peptides in which the single tyrosine residue either is nonsubstituted (Gastrin I) or is sulfated (Gastrin II). The three pairs have a common C-terminal tetradecapeptide sequence and differ only in the number of amino acids comprising the N-terminal portion of the molecule. The largest form contains 34 amino acid residues and is known as big gastrin or G-34. The other forms are the heptadecapeptide or little gastrin (G-17) and the tetradecapeptide or minigastrin (G-14). Other gastrin peptides which have been identified immunochemically but not characterized by chemical analysis include an amino terminal fragment of G-17, a molecule slightly larger than G-34 known as Component I, and a molecule with an apparent molecular weight similar to albumin known as big-big gastrin. None of these forms has apparent biological activity. In addition, synthetic preparations have been prepared of nonsulfated human G-34, G-17, and G-14, as well as shorter C-terminal fragments of gastrin which are not known to occur naturally.


Acid Secretion Gastric Acid Secretion Vary Chain Length Serum Gastrin Concentration Amino Terminal Fragment 
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  1. 1.
    Walsh JH, Grossman MI: Gastrin. New Eng J Med 292: 1324–1332, 1377–1384, 1975PubMedCrossRefGoogle Scholar
  2. 2.
    Walsh JH, Debas HT, Grossman MI: Pure human big gastrin: Immunochemical properties, disappearance half time, and acid stimulating action in dogs. J Clin Invest 54: 477–485, 1974.PubMedCrossRefGoogle Scholar
  3. 3.
    Walsh JH, Isenberg JI, Ansfield J, et al: Clearance and acid-stimulating action of human big and little gastrins in duodenal ulcer subjects. J Clin Invest 57: 1125–1131, 1976PubMedCrossRefGoogle Scholar
  4. 4.
    Dockray GJ, Taylor IL: Heptadecapeptide gastrin: measurement in blood by specific radioimmunoassay. Gastroenterology 71: 1114–1116, 1976Google Scholar
  5. 5.
    Feldman M, Richardson CT, Walsh JH: Mechanisms of acid secretory response to amino acid solutions in normal man. Clin Res 25: 467A, 1977Google Scholar
  6. 6.
    Fordtran JS, Walsh JH: Gastric acid secretion rate and buffer content of the stomach after eating: results in normal subjects and in patients with duodenal ulcer. J Clin Invest 52: 645–657, 1973PubMedCrossRefGoogle Scholar
  7. 7.
    Strunz UT, Walsh JH, Bloom SR, Thompson MR, Grossman MI: Lack of hepatic inactivation of VIP. Gastroenterology, 73: 768–771, 1977PubMedGoogle Scholar
  8. 8.
    Strunz UT, Walsh JH, Grossman MI: Removal of gastrin by various organs in dogs. Gastroenterology 74: 32–33, 1978PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • J. H. Walsh
    • 1
  1. 1.Department of MedicineU.C.L.A. Medical SchoolLos AngelesUSA

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