FULL LENGTH CDNA STRUCTURE AND DEDUCED AMINO-ACID SEQUENCE OF HUMAN 3-BETA-HYDROXY-5-ENE STEROID DEHYDROGENASE
FULL LENGTH CDNA STRUCTURE AND DEDUCED AMINO-ACID SEQUENCE OF HUMAN 3-BETA-HYDROXY-5-ENE STEROID DEHYDROGENASE
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DOI:
10.1210/mend-3-8-1310
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发表时间:
1989-08-01
影响因子:
--
通讯作者:
LABRIE, F
中科院分区:
文献类型:
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作者:
THE, VL;LACHANCE, Y;LABRIE, F
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.