Studies on 15-hydroxyprostaglandin dehydrogenase with various prostaglandin analogues
H Ohno, Y Morikawa, F Hirata - The Journal of Biochemistry, 1978 - academic.oup.com
H Ohno, Y Morikawa, F Hirata
The Journal of Biochemistry, 1978•academic.oup.comAbstract The NAD+-linked 15-hydroxyprostaglandin dehydrogenase (PGDH) of swine lung
was purified to a high specific activity by affinity chromatographies on prostaglandin (PG)-
and NAD+-Sepharose. The affinities of the enzyme for various synthetic analogues of PGA,
E, F, and I and their inhibitory effects on the enzymatic reaction were examined. The
modification of the alkyl side chain of PG, particularly at C-15 or C-16, reduced the affinity of
the enzyme for these PG analogues. Furthermore, 14-methyl-13, 14-dihydro-PGE1 and 16 …
was purified to a high specific activity by affinity chromatographies on prostaglandin (PG)-
and NAD+-Sepharose. The affinities of the enzyme for various synthetic analogues of PGA,
E, F, and I and their inhibitory effects on the enzymatic reaction were examined. The
modification of the alkyl side chain of PG, particularly at C-15 or C-16, reduced the affinity of
the enzyme for these PG analogues. Furthermore, 14-methyl-13, 14-dihydro-PGE1 and 16 …
Abstract
The NAD+-linked 15-hydroxyprostaglandin dehydrogenase (PGDH) of swine lung was purified to a high specific activity by affinity chromatographies on prostaglandin (PG)- and NAD+-Sepharose. The affinities of the enzyme for various synthetic analogues of PGA, E, F, and I and their inhibitory effects on the enzymatic reaction were examined. The modification of the alkyl side chain of PG, particularly at C-15 or C-16, reduced the affinity of the enzyme for these PG analogues. Furthermore, 14-methyl-13,14-dihydro-PGE1 and 16-cyclopentyl-ωtrinor-15-epi-PGE2 were potent inhibitors of PGDH.
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