Synthesis of the mating factor of Saccharomyces cerevisiae and its truncated peptides : the structure-activity relationship.

The mating factor of Saccharomyces cerevisiae, Trp-His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr, has been synthesized to confirm the structure of the natural mating factor. The tridecapeptide has the same biological activity as the natural mating factor. From the studies on the biological activity of its truncated peptide synthesized the minimum sequence of the peptide require for the mating factor was deduced to be as His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln.     

Ligand induced changes in stability and distribution of acetylcholine receptors on surface membranes of muscle cells

Distribution and stability of acetylcholine receptor (AChR) in cultured muscle cells was studied following the binding to these cells of concanavalin A (Con A) and specific antibodies against the receptor molecules. Con A (10 μg/ml) significantly slowed the rate of receptor degradation. In contrast, the rate of AChR degradation was enhanced 4-fold in the presence of the antibodies while the monovalent antibody fragments (Fab) were without effect. Divalent antibodies induced formation of large clusters on the surface of the muscle cultures within 2 h of incubation at 37°C. Monovalent antibody fragments and Con A had no effect on receptor distribution. It is suggested that receptor aggregation and turnover can be modulated by specific ligands acting at the cell surface.     

Relationship of prolactin receptors to concanavalin A binding

Concanavalin A, which binds to specific carbohydrate determinants on the cell surface, was used to investigate the binding of prolactin to its receptors in liver membranes from female rats. The binding of ¹²⁵I-labeled ovine prolactin to receptors was sharply inhibited by concanavalin A. This effect was reversed by the competitive sugar α-methyl-D-mannopyranoside and thus required the presence of specifically bound lectin. Concentrations of concanavalin A of up to 50 μg/ml caused a progressive decrease in the apparent affinity of the prolactin receptor for hormone. When higher concentrations were used, the number of available binding sites decreased. Concanavalin A-resistant receptors, about 30% of the total, had the same dissociation constant (K_d) as the controls. The binding of ¹²⁵I-labeled concanavalin A in the same membrane preparations showed the presence of two distinct types of concanavalin A binding. At low concentrations, the lectin bound with high affinity (K_d ≈ 6.6 · 10^?8 M). At high lectin concentrations, low affinity (K_d ≈ 6.7 · 10^?5 M) binding predominated. Since high affinity concanavalin A binding was saturated at 50 μg/ml, this class of binding most likely alters the affinity of the prolactin receptor for hormone; low affinity concanavalin A binding may mask prolactin receptors, making them inaccessible to the hormone.Binding sites for concanavalin A and prolactin appear to be independent but closely related since (i) concanavalin A did not displace bound prolactin from its receptor, and (ii) detergent-solubilized ¹²⁵I-labeled prolactin-receptor complexes bound to concanavalin A-Sepharose and were eluted by α-methyl-D-mannopyranoside.     

High affinity receptors for bombesin/GRP-like peptides on human small cell lung cancer

The binding of a radiolabeled bombesin analogue to human small cell lung cancer (SCLC) cell lines was investigated. (125I-Tyr4)bombesin bound with high affinity (Kd = 0.5 nM) to a single class of sites (2,000/cell) using SCLC line NCI-H446. Binding was reversible, saturable and specific. The pharmacology of binding was investigated using NCI-H466 and SCLC line NCI-H345. Bombesin and structurally related peptides, such as gastrin releasing peptide (GRP), but not other peptides, such as substance P or vasopressin, inhibited high affinity (125I-Tyr4)BN binding activity. Finally, the putative receptor, a 78,000 dalton polypeptide, was identified by purifying radiolabeled cell lysates on bombesin or GRP affinity resins and then displaying the bound polypeptides on sodium dodecylsulfate polyacrylamide gels. Because SCLC both produces bombesin/GRP-like peptides and contains high affinity receptors for these peptides, they may function as important autocrine regulatory factors for human SCLC.     

Variations in the levels of asterone and asterogenol, two steroids from the saponins of the starfish, Asterias vulgaris (Verrill)

The levels of two steroids, asterone 1 and asterogenol 4, obtained by hydrolysis of the crude asterosaponin mixture from the starfish Asterias vulgaris, were highest in winter and spring, then the steroid levels fell to their annual minima in July, after the spawning period. Levels also varied geographically, but the ratio of these steroids remained approximately constant.     

Induction of lordosis in the female hamster utilizing metabolites of progesterone

Progesterone, 6α-methyl-17α-OHP, and several progesterone metabolites were administered to ovariectomized, estrogen-primed female hamsters. Progesterone was most effective in the facilitation of sexual receptivity. 5α-Pregnan-3,20-dione was significantly more effective than the other progestins, which were no more effective than oil.     

Hemoglobins Austin and Waco: two hemoglobins with substitutions in the alpha 1 beta 2 contact region.

Hemoglobins (Hbs) Austin and Waco were detected by their electrophoretic migration on cellulose acetate (pH 8.4) and citrate agar (pH 6.2). By these methods, both variants migrated between Hbs A and F. Globin chain analysis at pH 8.6 indicated that the mutant β chain of Hb Austin was faster moving than the β^A chain; however, the mutant chain of Hb Waco was indistinguishable from the β^A chain by this technique. The two variants were isolated by ion-exchange column chromatography. Sequence studies demonstrated a substitution of serine (Hb Austin) and lysine (Hb Waco) for arginine at position 40 in the β chain. These mutations involve an amino acid residue in the α₁β₂ contact region, which, before this report, had been considered invariant in all hemoglobin sequences. Hb Austin was found to exist as dimers when oxygenated and as tetramers when deoxygenated. The equilibrium constant (K_d) for the tetramer to dimer transition was approximately 300 × 10^?6m, as calculated from sedimentation velocity studies. This variant also had high oxygen affinity, a much reduced heme-heme interaction, and a normal Bohr effect. The functional properties of Hb Waco were similar to those of Hb A.