Abstract
Homogenates and extracts of human placenta are able to desamidate glutamine by means of an enzyme which has the properties of glutaminase. Placental glutaminase is activated by phosphate. Its pH optimum lies at 9.0. A method for its assay in placental homogenate is described. It was found that the glutaminase activity decreases toward the end of pregnancy. At this time, the activity, expressed as Q NH 3 (N), amounts to 23.7 ± 6.7. Some quantitative aspects of glutaminase activity in the human placenta and kidney are discussed.
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