Inhibition of trypsin sulfhydryl reagents: Selective toxicities of organic mercury compounds

✍ Scribed by Cornelius W. Kreke

• Publisher: John Wiley and Sons
• Year: 1969
• Tongue: English
• Weight: 262 KB
• Volume: 58
• Category: Article
• ISSN: 0022-3549
• DOI: 10.1002/jps.2600580414

✦ Synopsis

Several mercury compounds including p-chloromercuribenzoate (PCMB) and phenylmercuric hydroxide (PMOH) were shown to bind with trypsin and to inhibit its proteolytic activity. None of the compounds showed activity when present in less than a 2,OOO:l molar ratio of compound to enzyme. Some were not effective even at a ratio of 300,OOO:l. A study of the stoichiometry of the inhibition shows that trypsin possesses three susceptible binding sites and that the mercury compounds differ not only in their affinities for these sites but also in their selectivities.

Keyphrases 0 Trypsin inhibition-mercury compounds 0 Proteolytic activity-trypsin inhibition analysis method Absorbance -protein binding analysis Colorimetric analysis-spectrophotometer 0 UV spectrophotometry-analysis * Bios Laboratories.