Full length cdna structure and deduced amino acid sequence of human 3β-hydroxy-5-ene steroid dehydrogenase

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Abstract

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.

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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

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