On the molecular basis of action of cytochalasin B.
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Biomedical subjects
Publications and source records attributed to S Lin.
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Data from a study of five stations on the Spoon River, Ill., during June 1971 through May 1973 were analyzed for compliance with Illinois Pollution Control Board's water quality standards of a geometric mean limitation of 200 fecal coliforms per 100 ml. This bacterial limit was achieved about 20% of the time during June 1971 through May 1972, and was never achieved during June 1972 through May 1973. Ratios of fecal coliform to total coliform are presented. By using fecal coliform-to-fecal streptococcus ratios to sort out fecal pollution origins, it was evident that a concern must be expressed not only for municipal wastewater effluents to the receiving stream, but also for nonpoint sources of pollution in assessing the bacterial quality of a stream.
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Cytochalasin B, an alkaloid that inhibits a wide variety of cellular movements, interacts with actomyosin, the contractile protein complex of striated muscle. This interaction causes a decrease in viscosity of the actomyosin complex and an inhibition of acto-heavy meromyosin ATPase activity of at least 60%. Cytochalasin B does not affect the viscosity of myosin nor the ATPase activity of heavy meromyosin, suggesting that the drug might interact directly with the actin moiety of the actomyosin complex. Indeed, as judged by viscometry, there is a strong interaction of cytochalasin B with actin, at nearly stoichiometric concentrations. Myosin appears to compete with cytochalasin for binding to actin.
Binding of lac repressor to 20 synthetic DNAs of high molecular weight with defined repeating sequences was investigated by competition experiments. Although none of these DNAs binds repressor as tightly as does lac operator, most do bind to a measurable extent. Their affinity for repressor varies greatly and is a function of both nucleotide composition and sequence. Poly(dC-dC).poly(dG-dC) competes for repressor 200-times less well than either poly(dA-dT).poly(dA-dT) or poly(dT-dT-dG).poly(dC-dA-dA). The other DNAs show a broad spectrum of affinities for repressor between these extremes. These results show that the lac repressor has affinity for, and can distinguish between, sequences distantly related to its operator.
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Penicillin induces partial depolarization and increased excitability of the neuronal membrane of crayfish stretch receptor. Such effects suggest that the epileptic focus created by the topical application of penicillin to the mammalian cerebral cortex may result from the lowering of the threshold for impluse initiation by excitatory synaptic action within the neuron population.
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