SEXUAL AGGLUTINATION IN SACCHAROMYCES CEREVISIAE.
Item
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Title
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SEXUAL AGGLUTINATION IN SACCHAROMYCES CEREVISIAE.
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Identifier
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AAI8401961
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identifier
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8401961
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Creator
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TERRANCE, KEVIN J.
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Contributor
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Peter Lipke
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Date
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1983
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Language
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English
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Publisher
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City University of New York.
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Subject
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Biology, Animal Physiology
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Abstract
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Treatment of either haploid mating type of Saccharomyes cerevisiae with the appropriate sex pheromone induced increased sexual agglutinability. Differences were noted between the two pheromones in the time and dose needed for maximal induction of their target cells. The action of (alpha)-factor was completely inhibited by cycloheximide, aminophylline, theophylline or tunicamycin, but only partially blocked by added cAMP. The action of a-factor was blocked by lesser concentrations of cycloheximide, but only if the cells were preincubated with the drug. a-Factor induction was only partially blocked by tunicamycin, even with a preincubation period. Overall, the results suggest asymmetry in the mechanisms of action of the two pheromones.;Cells exposed to (alpha)-factor for brief times (less than 30 sec.) became committed to induction of increased agglutinability, while morphogenesis requires continuous exposure to pheromone. a-Cells in G1 or in G2 of the cell cycle responded to (alpha)-factor induction with kinetics identical to that seen in unsynchronized cells.;Constitutively agglutinable and induced a-cells exhibited agglutinability across identical ranges of pH, ionic strength and temperature. All agglutinable combinations of cells, regardless of exposure to pheromone, were identical in response to a wide range of inhibitors.;Mechanical disruption of (alpha)-cells resulted in the solubilization of a molecular species with the predicted properties of (alpha)-agglutinin. This species behaved homogeneously in heat inactivation experiments, and was capable of blocking all possible agglutinins or a-cells.;Electrophoresis of purified (alpha)-agglutinin followed by staining with the new, ultrasensative silver technique (Goldman et al., 1981) revealed a total of 8 peptides, ranging from 33,000 to 120,000 daltons. This pattern persisted after two diverse purification steps. One of these steps, affinity chromatography onto lentil lectin, depended on carbohydrate residues that were only present in the 4 bands of highest molecular weight. This, along with supporting evidence, suggests a multi-subunit structure for the (alpha)-agglutinin.
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Type
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dissertation
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Source
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PQT Legacy CUNY.xlsx
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degree
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Ph.D.
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Program
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Biology
