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

Authors
Borhan-B; Hammock-B; Seifert-J; Wilson-BW
Source
Anal Bioanal Chem 1996 Feb; 354(4):490-492
NIOSHTIC No.
20032707
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 - 2 C(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).
Keywords
Chemical-analysis; Chemical-composition; Chemical-indicators; Chemical-properties; Chromatographic-analysis; Spectrographic-analysis; Chemical-extraction; Chemical-reactions; Chemical-structure; Chemical-synthesis
Contact
Borhan, B: Department of Chemistry, University of California, 95616 Davis, CA, USA
CODEN
ABCNBP
Publication Date
19960201
Document Type
Journal Article
Funding Amount
1055222
Funding Type
Cooperative Agreement
Fiscal Year
1996
NTIS Accession No.
NTIS Price
Identifying No.
Cooperative-Agreement-Number-U07-CCU-906162
Issue of Publication
4
ISSN
1618-2642
Source Name
Analytical and Bioanalytical Chemistry
State
CA; HI
Performing Organization
University of California - Davis
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