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Biomedical subjects

J D Hare

Publications and source records attributed to J D Hare.

At least 37 records · Page 2Linked to original sources
PubMed1976

Differential inactivation of the "L" and "Ly+" amino acid transport systems by a sulfhydryl reagent and a photo-affinity probe.

Using a substrate-stimulated amino acid efflux system, it has been shown that the "Ly+" and "L" amino acid transport systems of mouse embryo cells in culture are differentially inhibited by parachloromercuribenzene sulfonate (PCMB-S) and the photoaffinity probe 4-fluoro-3-nitrophenylazide (FNPA). Three types of evidence support the conclusion that these transport systems are mediated by separate carrier proteins. (1) The specificity of substrate-stimulated efflux is high for each system; (2) PCMB-S inhibits L-phenylalanine and L-leucine stimulated L-[3H]phenylalanine efflux with no effect on L-lysine stimulated L-[3H]lysine efflux, and (3) the photo-affinity probe FNPA inhibits L-lysine efflux with little effect on the L-phenylalanine-stimulated efflux.

4-Chloromercuribenzenesulfonate↗
PubMed1976

Inhibition of cell growth by near ultraviolet light photoproducts of tryptophan.

Exposure of dilute aqueous solutions of tryptophan to near UV light (320 to 390 nm) at subsolar levels yields fluorescent photoproducts capable of inhibiting the growth and differentiation of cultured mouse embryonic fibroblasts and fertilized sea urchin eggs. The ability of these cells to incorporate labelled precursors of protein, RNA, and DNA into their respective macromolecules was markedly inhibited by adding tryptophan preirradiated with near UV light to their incubation media. Thus the inhibition of growth and differentiation of these cells seems to result from a depression of their ability to synthesize macromolecules in the presence of the photoproducts.

Animals↗
PubMed1975

Polyoma virus strain with enhanced synthesis of capsid protein.

A study of the immunochemical characteristics and the synthesis of the capsid proteins of two polyoma virus strains (3049 and 1pS) was carried out to determine the mechanism responsible for the unique accumulation of those structural polypeptides in the cytoplasm of cells infected with the 3049 strain. Antisera prepared against disaggregated virus peptides and whole virus were used to measure the quantity of virus-specific antigens in cells infected by the two strains by using an indirect radioimmunoassay technique. The 3049-infected mouse embryo cells were found to contain several-fold more antibody-binding material than those infected with the 1pS strain. Furthermore, the cytoplasmic fraction of 3049-infected cells also contained more antibody-binding activity, supporting the hypothesis that the phenotype of the 3049 virus (cytoplasmic capsid protein) was a reflection of the increased synthesis of the capsid polypeptides.

Amanitins↗