In vitro biosynthesis and core glycosylation of the histidine-rich protein of Plasmodium lophurae

1983 ◽  
Vol 9 (4) ◽  
pp. 351-362 ◽  
Author(s):  
Roslyn Feder ◽  
Günter Blobel
1973 ◽  
Vol 17 (3) ◽  
pp. 617
Author(s):  
K. S. Mandhare ◽  
G. T. Dimopoullos ◽  
L. T. Hart

1969 ◽  
Vol 18 (5) ◽  
pp. 657-661 ◽  
Author(s):  
William G. Brundage ◽  
Christopher Marie Hyland ◽  
G. T. Dimopoullos

1968 ◽  
Vol 46 (8) ◽  
pp. 749-757 ◽  
Author(s):  
H. R. Raud ◽  
R. Hobkirk

The sulfurylation of estrone-6,7-3H, estradiol-17β-6,7-3H, and dehydroisoandrosterone-4-14C by laying hen liver, oviduct, and vaginal preparations was investigated. Purification and product identification included ether and ethyl acetate extraction, paper chromatography, and isotope dilution, before and after hydrolysis with a sulfatase preparation.The esterifying enzymes were found in the 105 000 × g supernatants of the three tissues. The liver preparation was many times more active in steroid sulfate synthesis than the corresponding oviduct or vaginal fractions. Sulfurylation of dehydroisoandrosterone displayed the same cofactor, pH, and temperature requirements as did that of estrone and estradiol-17β. The degree of dehydroisoandrosterone sulfate synthesis was considerably lower than that of the estrogens, however. It is suggested that the laying hen possesses an enzyme system which is more efficient for the sulfurylation of estrogens than of other steroids such as dehydroisoandrosterone.


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