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Biomedical subjects

J Marr

Publications and source records attributed to J Marr.

At least 55 records · Page 3Linked to original sources
PubMed1980

A sudden decline in ampicillin resistance in Salmonella typhimurium.

Starting in 1975, an abrupt decline in ampicillin resistance of Salmonella typhimurium (the most common and antibiotic-resistant serotype) occurred in New York City. The present lower rate of 5% to 7.9% at our hospitals represents a return to the 1965 level. At the same time, the ampicillin resistance in S typhimurium from calves and other farm animals from upper New York State, which has been rising since 1972, has reached 75%. Substantial differences between levels of resistance in Escherichia coli from animals and humans were also noted. The divergence of the trends in S typhimurium from these two sources in New York State suggests a substantial degree of separation of the respective reservoirs of Salmonella and of antibiotic resistance.

Ampicillin↗
PubMed1976

Adenosine cyclic 3',5'-monophosphate-dependent protein kinase from human platelets.

A single cyclic AMP-dependent protein kinase (EC 2.7.1.37) has been isolated from human platelets by using DEAE-cellulose ion-exchange chromatography and Sephadex G-150 gel filtration. The molecular weight of the protein kinase was estimated to be 86 490. In the presence of cyclic AMP, the protein kinase could be dissociated into a catalytic subunit of molecular weight 50 000, and either one regulatory subunit of molecular weight 110 000 or two regulatory subunits of molecular weights 110 000 and 38 100, depending on the pH used. Recombination of either of the regulatory subunits with the catalytic subunit restored cyclic AMP-dependency in the catalytic subunit. The apparent Km for ATP in the presence of 10 muM Mg2+ was 4 muM (plus cyclic AMP) and 4.3 muM (minus cyclic AMP). The concentration of cyclic AMP needed for half-maximal stimulation of the protein kinase was 0.172 muM and apparent dissociation constants of 3.7 nM (absence of MgATP) and 0.18 muM (presence of MgATP) were exhibited by the "protein kinase-cyclic AMP complex". The enzyme required Mg2+ for maximum activity and showed a pH optimum of 6.2 with histone as substrate. In addition to four major endogenous platelet protein acceptors of apparent molecular weights 45 000, 28000, 18 500, and 11 100, the platelet protein kinase also phosphorylated the exogenous acceptor proteins thrombin, collagen and histone, all capable of inducing platelet aggregation. Prothrombin, a nonaggregating agent, was not phosphorylated.

Binding Sites↗