
Occurrence of O‐phosphorylated 2‐keto‐3‐deoxyoctonate in the lipopolysaccharide of Bacteroides gingivalis
Author(s) -
Kumada Hidefumi,
Watanabe Kiyoko,
Umemoto Toshio,
Haishima Yuji,
Kondo Seiichi,
Hisatsune Kazuhito
Publication year - 1988
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1988.tb02972.x
Subject(s) - chemistry , lipopolysaccharide , periodate , bacteroides , hydrolysate , thiobarbituric acid , phosphorylation , biochemistry , bacteria , biology , enzyme , hydrolysis , lipid peroxidation , endocrinology , genetics
Periodate‐thiobarbituric acid reaction‐positive substances were found in the strong acid hydrolysates of the lipopolysaccharide (LPS) from Bacteroides gingivalis 381. They were not identical to 2‐keto‐3‐deoxyoctonate (KDO) in high‐voltage paper electrophoresis (HVPE), their electrophoretic mobilities relative to KDO being 1.54 and 1.80, respectively. Alkaline phosphatase treatment and HVPE demonstrated that they are some kind of O‐phosphorylated derivatives of KDO; in particular, the slow‐moving component is identical, at least in HVPE, to 5‐ O ‐phosphoryl‐KDO isolated from the strong acid hydrolysates of Bordetella pertussis (phase I) LPS.