3,3,3-TRIFLUORO-2-DIAZOPROPIONYLCHLORIDE PLEASE INQUIRE

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Affinity labeling the bovine gallbladder cholecystokinin receptor using a battery of probes Affinity labeling the bovine gallbladder cholecystokinin receptor using a battery of probes. Schjoldager, Birgit; Powers, Stephen P.; Miller, Laurence J. (Gastroenterol. Res. Unit, Mayo Clin. Found., Rochester, MN 55905, USA). Am. J. Physiol., 255(5, Pt. 1), G579-G586 (English) 1988. CODEN: AJPHAP. ISSN: 0002-9513. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Section cross-reference(s): 6, 9, 34 The bovine gallbladder muscularis cholecystokinin (CCK) receptor was characterized by using long (125I-Bolton-Hunter-CCK-33) and short {125I-D-Tyr-Gly-[(Nle28,31)CCK-(26-33)]} probes chem.In this experiment, several chemicals are used like 59733-92-5 cross-linkable through their amino-terminal amino groups and by monofunctional probes with their photolabile moieties at their amino terminus {2-diazo-3,3,3-trifluoropropionyl-125I-D-Tyr-Gly-[(Nle28,31)CCK-(26-33)]} and carboxyl terminus {125I-D-Tyr-Gly-[(Nle28,31,pNO2-Phe33)CCK-(26-33)]}, that span the receptor-binding region. Each of these bound specifically and saturably to a prepn. enriched in plasma membranes from bovine gallbladder muscularis (mean inhibitor consts.: 5.2, 1.1, 0.8, and 1.8 nM, resp.). A major Mr 70,000-85,000 band was specifically and reproducibly labeled with the appropriate apparent affinity by each of the probes, whereas labeling of minor bands of Mr 40,000-50,000, 92,000, 120,000, and 200,000 was dependent on cross-linker type or concn. These observations support the identification of the Mr 70,00-85,000 protein as the bovine gallbladder CCK-binding subunit and, since this is a different size from the pancreatic CCK-binding subunit, thid provides biochem. evidence for mol. heterogeneity of peripheral CCK receptors. .