. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. G. C. CHIN ET AL. 50 100 Time at 0°C (min) 200 10000 £ D- 8000- 6000 .3 oa o S 4000- O. on 2000 20 40 60 8< Time at 25°C (min) 100 120 Figure 1. Time course of FMRFamide receptor binding in SQM. For the upper and lower figures respectively, ['25I]-daYFnLRFa ( and nA/) was incubated with SQM (50 and 10 ^g protein) at 0° and 25°C. The total and nonspecific binding were determined in triplicate in single experiments at the times indicated, and the specific binding (± SEM) is plotted against time. (Lake el ai. 1991
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. G. C. CHIN ET AL. 50 100 Time at 0°C (min) 200 10000 £ D- 8000- 6000 .3 oa o S 4000- O. on 2000 20 40 60 8< Time at 25°C (min) 100 120 Figure 1. Time course of FMRFamide receptor binding in SQM. For the upper and lower figures respectively, ['25I]-daYFnLRFa ( and nA/) was incubated with SQM (50 and 10 ^g protein) at 0° and 25°C. The total and nonspecific binding were determined in triplicate in single experiments at the times indicated, and the specific binding (± SEM) is plotted against time. (Lake el ai. 1991; Malin ct a/., 1990a, b: Malin et 1993; Tang et ai. 1984; Yang el ai. 1985); for reviews, see Raffa (1988) and Rothman (1992). The actions of FMRFamide and the mammalian FMRFamide-related peptide Neuropeptide FF (NPFF) appear to be mediated through binding to NPFF receptors in rats (Allard et ai, 1989; Payza et ai. 1993). Despite numerous studies of the cellular effects of FMRFamide and related peptides, little is known about the receptors for these ligands. An in vitro radioligand binding assay was developed and used to characterize the receptor in Helix nervous tissue and heart (Payza, 1987; Payza et ai. 1989). These studies indicated that [I25I]- daYFnLRFa binds in a reversible, saturable, and specific manner to FMRFamide receptors of high (13 nM) and low (250 nA/) affinity in Helix brain. This approach has been extended to include characterization of the rat spinal cord receptor for NPFF (Allard et al., 1989; Payza and Yang, 1993). Nevertheless, purified FMRFamide receptor protein and sequence information are necessary to develop specific molecular probes with which to study receptor expression, distribution, and diversity. Thus, we sought to identify a source of molluscan nervous tissue in which FMRFa vie receptors could be studied, and from which the recep rs could be solubilized and eventually purified. Here \ e describe the characterization, effector-cou- pl
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Keywords: ., bookauthorlilliefrankrat, booksubjectbiology, booksubjectzoology
