Enzymes from Bovine Placenta and Seminal Vesicles That Oxidize D(—)-l,2-Propanediol and Other Polyols: Their Possible Relation to Fructose Formation1
- 1 March 1964
- journal article
- research article
- Published by The Endocrine Society in Endocrinology
- Vol. 74 (3) , 429-439
- https://doi.org/10.1210/endo-74-3-429
Abstract
Using chromatographic methods, soluble proteins displaying D(—)-l,2- propanediol: NADP oxidoreductase activity have been purified 50- to 60-fold from bovine placental tissue and from bovine seminal vesicle. The enzymes, which have similar chromatographic behavior, show stereospecificity for the D-forms of the substrates tested. They catalyze the following reversible reactions : D-l, 2-propanediol→ D-lactaldehy de, glyceroL →D-glyceraldehyde, D-sorbitol→D-glucose. Both enzymes are active over a wide pH range and are strongly inhibited by p-mercuribenzoate and by some heavy metals. The reaction kinetics do not follow the Michaelis-Menten equation when the aldehydes are used as substrates. It is proposed that the main physiological function of these enzymes is to catalyze the transformation of D-glucose to D-sorbitol, an intermediate in D-fructose formation. (Endocrinology74: 429, 1964)Keywords
This publication has 1 reference indexed in Scilit:
- Le mécanisme de la formation du fructose séminal et du fructose foetalBiochimica et Biophysica Acta, 1959