PURIFICATION AND PROPERTIES OF ALDOSE REDUCTASES FROM PLACENTA AND SEMINAL VESICLE OF SHEEP

NADP-dependent aldose reductase has been purified 35-fold from ovine placenta and 70-fold from ovine seminal vesicles. The purified placentate enzyme still showed two precipitation arcs when tested by immunodiffusion and immunoelectrophoresis. The seminal vesicle preparation appeared to be homogeneous, using the same procedures. There was not immunological cross reaction between the enzymes purified from the two sexes of the same species. The kinetic behaviour of the two enzymes were very similar, with high reactivity towards aldehydes as substrates, but low reactivity towards the corresponidng alcohols. With aldehydes as substrates both enzymes showed marked deviation from linearity in the Lineweaver-Burk plot, indicating substrate activation. © 1969.