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  • Title: Differences in receptor binding and stability to enzymatic digestion between CCK-8 and CCK-58.
    Author: Reeve JR, McVey DC, Bunnett NW, Solomon TE, Keire DA, Ho FJ, Davis MT, Lee TD, Shively JE, Vigna SR.
    Journal: Pancreas; 2002 Oct; 25(3):e50-5. PubMed ID: 12370550.
    Abstract:
    INTRODUCTION AND AIMS: It has been proposed that distinct tertiary structures of the C-terminus of CCK-8 and CCK-58 result in differences in stimulation of pancreatic amylase secretion. Binding of CCK-8 and CCK-58 to CCK-A and CCK-B receptors and stability to enzymatic digestion were used as independent probes for tertiary structure of the C-terminus. METHODOLOGY: Canine CCK-58 was purified from intestinal extracts and CCK-8 was purchased. Their amounts were determined by amino acid analysis. The effect of tertiary structure on receptor binding at CCK-A receptors and CCK-B receptors was evaluated using membrane preparations from mouse pancreas and brain. The influence of C-terminal tertiary structure on stability to enzymatic digestion was evaluated by reacting CCK-8 and CCK-58 with endopeptidase 24:11. RESULTS: CCK-58 was three times more potent than CCK-8 for binding mouse pancreatic membrane CCK-A receptors and equipotent to CCK-8 for binding mouse brain CCK-B receptors. CCK-8 was readily digested by endopeptidase 24:11, whereas CCK-58 was not. CONCLUSIONS: The results strongly support the hypothesis that differences in tertiary structure of the carboxyl terminus of CCK-8 and CCK-58 influence receptor binding and stability to enzymatic digestion.
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