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Chemical Compound Review

PCMB     sodium (4-carboxylatophenyl)mercury hydrate

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Disease relevance of p-Chloromercuribenzoic acid

  • Cell-free extracts of E. coli strains hosting the thiol-beta-lactamase gene possess a p-chloromercuribenzoate-sensitive beta-lactamase activity [1].
  • Challenge of human or murine melanoma cells with sodium arsenite, heavy metals (Zn2+, Cu2+ and Cd2+), or thiol-reactive agents (p-chloromercuribenzoate and iodoacetamide) induced the synthesis of four stress proteins with molecular masses of 100, 90, 72 (a doublet), and 32 (human) or 34 (murine) kDa [2].
  • Since the acyl-enzyme mechanism is not annihilated by pCMB derivatization, it is proposed that basically, and like all the other DD-peptidases/penicillin-binding proteins so far characterized, the Streptomyces K15 DD-peptidase is an active-site-serine enzyme [3].
  • The H2-oxidation, H2-production and H-3H-exchange activities of the periplasmic hydrogenase from Desulfovibrio vulgaris (Hildenborough) were almost completely abolished by Hg(II) and the organic mercurials p-chloromercuribenzoate (pCMB) and p-hydroxymercuriphenylsulphonate [4].
  • Among a wide range of potential selective agents examined, sodium p-hydroxymercuribenzoate successfully enriched for mutants of Synechocystis sp. strains PCC 6714 and 6803 defective in photosynthesis [5].

High impact information on p-Chloromercuribenzoic acid


Chemical compound and disease context of p-Chloromercuribenzoic acid


Biological context of p-Chloromercuribenzoic acid


Anatomical context of p-Chloromercuribenzoic acid


Associations of p-Chloromercuribenzoic acid with other chemical compounds


Gene context of p-Chloromercuribenzoic acid


Analytical, diagnostic and therapeutic context of p-Chloromercuribenzoic acid


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