Methyl and phenyl esters and thioesters of carboxylic acids as surrogate substrates for microassay of proteinase K esterase activity

Babak Borhan, Bruce Hammock, Josef Seifert, Barry W. Wilson

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The development of a microassay for proteinase K esterase activity with carboxylic acid esters is reported using novel substrates of the general formula R-C(O)-XR′. Highest rates of hydrolysis have been obtained with the O-phenyl esters CH3(CH2)n = 1-2-S-(CH2)n=1-2C(O)-O-phenyl and their thioester analogs in studies where R, X and R′ have been varied. The phenol release has been measured with 4-aminoantipyrine and potassium ferricyanide to determine the rates of O-phenyl ester hydrolyses. Thioester hydrolyses have been monitored continuously with 5,5′-dithio-bis (2-nitrobenzoic acid).

Original languageEnglish (US)
Pages (from-to)490-492
Number of pages3
JournalFresenius' Journal of Analytical Chemistry
Volume354
Issue number4
StatePublished - Feb 2 1996

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Endopeptidase K
Esterases
Carboxylic Acids
Hydrolysis
Esters
Substrates
Ampyrone
Nitrobenzoates
Phenol

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Analytical Chemistry

Cite this

Methyl and phenyl esters and thioesters of carboxylic acids as surrogate substrates for microassay of proteinase K esterase activity. / Borhan, Babak; Hammock, Bruce; Seifert, Josef; Wilson, Barry W.

In: Fresenius' Journal of Analytical Chemistry, Vol. 354, No. 4, 02.02.1996, p. 490-492.

Research output: Contribution to journalArticle

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