Polyclonal antibodies raised against 3β-hydroxyste-roid dehydrogenase isolated from human placenta were used to screen a λgt11 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 3β-hydroxyste-roid dehydrogenase is the enzyme catalyzing the formation of all classes of hormonal steroids, the availability of the 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. © 1989 by The Endocrine Society.
Mendeley helps you to discover research relevant for your work.
CITATION STYLE
The, V. L., Lachance, Y., Labrie, C., Leblanc, G., Thomas, J. L., Strickler, R. C., & Labrie, F. (1989). Full length cdna structure and deduced amino acid sequence of human 3β-hydroxy-5-ene steroid dehydrogenase. Molecular Endocrinology, 3(8), 1310–1312. https://doi.org/10.1210/mend-3-8-1310