Inhibition of Growth of Pediococcus cerevisiae by Polycyclic Hydrocarbon-Cysteine Conjugates

Frendo, J; Wood, John L.

doi:10.3181/00379727-145-37835

Cited by 2 publications

(1 citation statement)

References 3 publications

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“…The inhibitory effect of these arylcysteines was partially reversed by the natural amino acids, previously shown by Bucovaz et al (1970) to be competitive with these particular S-substituted cysteines. Also Frendo and Wood (1974) reported that certain aromatic hydrocarbon cysteine conjugates inhibited the growth of Pediococcus cerevisiae. The inhibitory effects in this organism were also partially reversed by amino acids previously shown to be competitive with the analogue in an in vitro rat liver system.…”

Section: Resultsmentioning

confidence: 99%

Quantification of the role of smoking and chewing tobacco in oral, pharyngeal, and oesophageal cancers

Jayant¹,

Balakrishnan²,

Sanghvi³

et al. 1977

Br J Cancer

120

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Summary.-Evidence is presented which indicates that S-(1,2,3,4-tetrahydro-2-hydroxy-l-naphthyl)-L-cysteine (THN-cysteine), formed by the reaction of 1,2-epoxy-THN with cysteine, can be incorporated into protein. The position of incorporation of THN-cysteine into protein would depend on whether the epoxide of THN reacts with cysteinyl-tRNACYs or with cysteine. In both cases, the mechanism of incorporation of THN-cysteine into protein is the same as for the natural amino acids. For example, the incorporation of THN-cysteinyl-tRNACYs is stimulated by Poly-UG, the code for tRNACys, and would be expected to be substituted for cysteine in protein being synthesized, whereas THN-cysteine not previously esterified to tRNA is activated by the isoleucyl-and valyl-RNA synthetases, and its incorporation is stimulated by Poly-AU and Poly-UG, respectively. Consequently, in this case, THN-cysteine would substitute for isoleucine and valine during protein synthesis.

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Section: Resultsmentioning

confidence: 99%

Quantification of the role of smoking and chewing tobacco in oral, pharyngeal, and oesophageal cancers

Jayant¹,

Balakrishnan²,

Sanghvi³

et al. 1977

Br J Cancer

120

View full text Add to dashboard Cite

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Mechanism for the incorporation of S-(1,2,3,4-tetrahydro-2-hydroxy-1-naphthyl)-L-cysteine into protein

Morrison¹,

Whybrew²,

Sobhy³

et al. 1977

Br J Cancer

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Summary.-A transplantable reticulum-cell sarcoma induced by Rauscher virus (RV) in (C57BL/6 x DBA/2)F1 (BDF1) mice was grown in tissue culture. Four separate cell lines were established, all of which grew predominantly in suspension. The doubling time of the cells from these cultures ranged from 17 to 32 h. Each culture continued to replicate RV, as indicated by the infectivity in newborn mice of all fluids tested up to the 75th passage. Since the morphological appearance of the cells in vitro was consistent with that of proerythroblasts, all cultures were tested for their ability to differentiate along the erythrocytic line under the influence of dimethylsulphoxide (DMSO). One of the cultures produced small quantities of haemoglobin independently of DMSO. Another was shown to produce haemoglobin, as well as to take up 59Fe and incorporate it into haem, only in the presence of DMSO. The 2 remaining cultures failed to produce haemoglobin, either spontaneously or in the presence of DMSO. Cells from each of the RV-induced cultures, when inoculated back into BDF1 mice, induced typical reticulum-cell sarcomas, without in vivo evidence of erythroid differentiation. In contrast, 2 morphologically identical but non-infectious cell lines derived from Friend virus-induced reticulumcell sarcomas did not show erythroid differentiation in vivo or in vitro, either in the absence or presence of DMSO.

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Inhibition of Growth of Pediococcus cerevisiae by Polycyclic Hydrocarbon-Cysteine Conjugates

Cited by 2 publications

References 3 publications

Quantification of the role of smoking and chewing tobacco in oral, pharyngeal, and oesophageal cancers

Quantification of the role of smoking and chewing tobacco in oral, pharyngeal, and oesophageal cancers

Mechanism for the incorporation of S-(1,2,3,4-tetrahydro-2-hydroxy-1-naphthyl)-L-cysteine into protein

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