Human placental alcohol dehydrogenase.
Alcohol dehydrogenase derived from the term human placenta was investigated in the 104,000xg supernatant fraction. Kinetic experiments yielded an average Vmax of 6.1 units, a Km of  5X10(-3)M and optimum activity at pH 10.0. Electrophoresis at pH 9.6 in glycine buffer showed four bands, however only two bands were observed at pH 8.6. Properties of this placental enzyme may be unique and its participation in the overall metabolic function of this tissue is unclear.
Human placental alcohol dehydrogenase. Alcohol dehydrogenase derived from the term human placenta was investigated in the 104,000xg supernatant fraction. Kinetic experiments yielded an average Vmax of 6.1 units, a Km of  5X10(-3)M and optimum activity at pH 10.0. Electrophoresis at pH 9.6 in glycine buffer showed four bands, however only two bands were observed at pH 8.6. Properties of this placental enzyme may be unique and its participation in the overall metabolic function of this tissue is unclear.