Purification and characterization of novel sulfotransferase obtained from Klebsiella K-36, an intestinal bacterium of rat.

Abstract:

:A novel type of sulfotransferase was purified from Klebsiella K-36, an intestinal bacterium of rat. The enzyme (M(r) 160,000) is composed of two subunits (M(r) 73,000) with pI and optimal pH values of 5.3 and 10-10.5, respectively. The apparent Km for PNS (p-nitrophenyl sulfate) using phenol as an acceptor and that for phenol using PNS as a donor substrate were determined to be 0.11 and 0.66 mM, respectively. The enzyme is activated by magnesium ion and inhibited by EDTA.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Kim DH,Kim HS,Kobashi K

doi

10.1093/oxfordjournals.jbchem.a123921

keywords:

subject

Has Abstract

pub_date

1992-10-01 00:00:00

pages

456-60

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

112

pub_type

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