Full Length cDNA Structure and Deduced Amino Acid Sequence of Human β-Hydroxy-5-Ene Steroid Dehydrogenase

Abstract

Polyclonal antibodies raised against 3.beta.-hydroxysteroid dehydrogenase isolated from human placenta were used to screen a .lambda.gt11 expression cDNA library from the same tissue. The protein deduced from cDNA sequences contains 372 amino acids with a calculated mol wt of 42,216. Since 3.beta.-hydroxysteroid dehydrogenase is the enzyme catalyzing the formation of all classes of hormonal steroids, the availability of cDNA encoding this enzyme opens new possibilities for a detailed investigation of the factors regulating the expression and activity of this crucial enzyme in adrenal, gonadal as well as peripheral tissues.