-transparent.png){kind=logo}
15-Hydroxy-prostaglandin-dehydrogenase was purified 3 to 5 fold and with almost 100% yield from swine lungs by a novel method of precipitation with Rivanol after which it was further purified (8-10 fold) by gel-filtration. The optimal stability parameters of the purified enzyme preparation were determined and the behaviour of PGDH in polyacrylamide-gel-electrophoresis was studied by local enzyme detection. The enzyme seems to be composed of subunits. KM values of PGDH with respect to NAD, PGE2 and PGF2alpha were found to be 0.27, 0.017 and 0.038 mM, respectively.
Related Publications
P Tolnay, and
A Divald, and
G Cseh
April 1972,
Biochemical and biophysical research communications,
P Tolnay, and
A Divald, and
G Cseh
August 1975,
European journal of biochemistry,
P Tolnay, and
A Divald, and
G Cseh
March 1974,
Prostaglandins,
P Tolnay, and
A Divald, and
G Cseh
April 1970,
Experientia,
P Tolnay, and
A Divald, and
G Cseh
March 1971,
Acta physiologica Scandinavica,
P Tolnay, and
A Divald, and
G Cseh
May 1972,
Prostaglandins,
P Tolnay, and
A Divald, and
G Cseh
November 1974,
FEBS letters,
P Tolnay, and
A Divald, and
G Cseh
July 1976,
Biochemical pharmacology,
P Tolnay, and
A Divald, and
G Cseh
August 1974,
Prostaglandins,
P Tolnay, and
A Divald, and
G Cseh
November 1982,
The Journal of biological chemistry,
