Leydig cell andΔ 5-3β-hydroxysteroid dehydrogenase activity in the testis of toad (Bufo melanostictus) following cold exposuredehydrogenase activity in the testis of toad (Bufo melanostictus) following cold exposure

1982 ◽  
Vol 38 (6) ◽  
pp. 692-693 ◽  
Author(s):  
P. B. Patra ◽  
N. M. Biswas
Keyword(s):  
Dehydrogenase Activity ◽  
Cold Exposure ◽  
Leydig Cell ◽  
Hydroxysteroid Dehydrogenase ◽  
Bufo Melanostictus ◽  
Toad Bufo

3β-HYDROXYSTEROID DEHYDROGENASE IN THE FOETAL MOUSE LEYDIG CELL

1964 ◽  
Vol 31 (1) ◽  
pp. 63-NP ◽  
Author(s):  
A. H. BAILLIE ◽  
K. GRIFFITHS
Keyword(s):  
Dehydrogenase Activity ◽  
Leydig Cell ◽  
Hydroxysteroid Dehydrogenase ◽  
Hydroxysteroid Dehydrogenases ◽  
Weak Activity ◽  
Mouse Leydig Cell

SUMMARY Five male foetal mice were killed daily from the 11th day of gestation until term, the 21st day. Sections of testis from every animal were incubated with three steroid substrates to demonstrate 3β-hydroxysteroid dehydrogenase histochemically. The substrates were (1) 3β-hydroxypregn-5-en-20-one (pregnenolone), (2) 3β,17α-dihydroxypregn-5-en-20-one (17α-hydroxypregnenolone), and (3) 3β-hydroxyandrost-5-en-17-one (DHA). With pregnenolone as substrate 3β-hydroxysteroid dehydrogenase activity was demonstrable from the 11th day, when the testis is first histologically recognizable, until the end of gestation. Using 17α-hydroxypregnenolone, no 3β-hydroxysteroid dehydrogenase activity was present in the foetal testis. With DHA as substrate weak activity was first seen in the testis of the 15-day foetal mouse, and increased steadily thereafter. These findings are thought to support the concept of substrate-specific 3β-hydroxysteroid dehydrogenases.

3β-HYDROXYSTEROID DEHYDROGENASE ACTIVITY IN THE MOUSE LEYDIG CELL

1964 ◽  
Vol 29 (1) ◽  
pp. 9-17 ◽  
Author(s):  
A. H. BAILLIE ◽  
K. GRIFFITHS
Keyword(s):  
Dehydrogenase Activity ◽  
Leydig Cell ◽  
Age Groups ◽  
Hydroxysteroid Dehydrogenase ◽  
Postnatal Life ◽  
Dehydrogenase Enzyme ◽  
High Level ◽  
Mouse Leydig Cell

SUMMARY One hundred and thirty-two male Swiss white mice were killed in batches of twelve, between birth and the end of the 10th week of postnatal life inclusive, a total of eleven groups. Sections of testis from every animal were incubated with three steroid substrates to demonstrate 3β-hydroxysteroid dehydrogenase histochemically. The substrates were (1) 3β: 17α-dihydroxypregn-5-en-20-one (17α-hydroxypregnenolone), (2) 3β-hydroxypregn-5-en-20-one (pregnenolone) and (3) 3β-hydroxyandrost-5-en-17-one (DHA). When 17α-hydroxypregnenolone was used as a substrate no 3β-hydroxysteroid dehydrogenase activity was demonstrable in the testis until the end of the 10th week of postnatal life. With pregnenolone as a substrate 3β-hydroxysteroid dehydrogenase activity was demonstrable throughout the age groups studied. It was present at birth and increased progressively until the end of the 6th week of postnatal life. Thereafter the activity decreased progressively during the ensuing 4 weeks. With DHA as substrate activity was again demonstrable in all age groups studied and increased progressively from birth until the end of the 7th week of postnatal life after which a relatively constant high level was maintained. On the basis of these findings the existence of more than one 3β-hydroxysteroid dehydrogenase enzyme is postulated, each enzyme being substrate specific.

THE INFLUENCE OF HAEMOGLOBIN-S AND G6PD DEFICIENCY ON THE ACTIVITY OF THE 17β-HYDROXYSTEROID DEHYDROGENASE OF INTACT HUMAN ERYTHROCYTES

1974 ◽  
Vol 75 (4) ◽  
pp. 793-800
Author(s):  
A. O. Sogbesan ◽  
O. A. Dada ◽  
B. Kwaku Adadevoh
Keyword(s):  
Enzyme Activity ◽  
Dehydrogenase Activity ◽  
Sex Steroids ◽  
G6pd Deficiency ◽  
Incubation Medium ◽  
Hydroxysteroid Dehydrogenase ◽  
G6pd Activity ◽  
Reverse Transformation ◽  
Oxidative Transformation ◽  
Haemoglobin S

ABSTRACT The 17β-hydroxysteroid dehydrogenase activity in intact erythrocytes of Nigerian patients, in particular with regard to haemoglobin genotypes and G6PD* activity was studied. The G6PD activity of the erythrocyte did not affect the oxidative transformation of testosterone to androstenedione and of oestradiol to oestrone. The reduction (reverse transformation) was inhibited in G6PD-deficient erythrocytes but this inhibition was offset by the addition of 0.025 m glucose to the incubation medium. The per cent oxidation transformation of testosterone was higher in Hb-AA than in Hb-SS erythrocytes. It is suggested that the differences may be a result of either lower enzyme activity in the Hb-SS erythrocytes or of differences in the uptake and possibly binding of sex steroids by intact Hb-SS and Hb-AA erythrocytes.

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