PURIFICATION AND PROPERTIES OF A HIGHLY-ACTIVE ORGANOPHOSPHORUS ACID ANHYDROLASE FROM ALTEROMONAS-UNDINA

Authors
CHENG TC HARVEY SP STROUP AN
Citation
Tc. Cheng et al., PURIFICATION AND PROPERTIES OF A HIGHLY-ACTIVE ORGANOPHOSPHORUS ACID ANHYDROLASE FROM ALTEROMONAS-UNDINA, Applied and environmental microbiology, 59(9), 1993, pp. 3138-3140
Citations number
11
Categorie Soggetti
Microbiology,"Biothechnology & Applied Migrobiology
Journal title
Applied and environmental microbiology → ACNP
ISSN journal
00992240
Volume
59
Issue
9
Year of publication
1993
Pages
3138 - 3140
Database
ISI
SICI code
0099-2240(1993)59:9<3138:PAPOAH>2.0.ZU;2-7
Abstract
A highly active organophosphorus acid anhydrolase from Alteromonas und ina was purified to homogeneity and found to be composed of a single p olypeptide chain with a molecular weight of 53,000. With diisopropylfl uorophosphate as a substrate, the purified enzyme has a specific activ ity of approximately 575 mumol/min/mg of protein. The enzyme has optim um activity at pH 8.0 and 55-degrees-C and is stimulated by sulfhydryl reducing agents and manganese. It is capable of rapidly hydrolyzing a wide range of nerve agents and several chromogenic phosphinates.