scholarly journals Polytopic Cation Receptors. III. Di- and Triloop Crown Hosts Having Aromatic Junctions. Synthesis, Cation Extraction, and Solid Complex Formation

1990 ◽  
Vol 63 (12) ◽  
pp. 3670-3677 ◽  
Author(s):  
Edwin Weber ◽  
Konstantinos Skobridis ◽  
Mikio Ouchi ◽  
Tadao Hakushi ◽  
Yoshihisa Inoue
1973 ◽  
pp. 442-445 ◽  
Author(s):  
Juziro Nishijo ◽  
Isamu Imanishi ◽  
Genzo Hashizume ◽  
Toshio Kinugasa

1971 ◽  
Vol 44 (8) ◽  
pp. 2035-2038 ◽  
Author(s):  
Toshio Kinugasa ◽  
Juziro Nishijo ◽  
Genzo Hashizume ◽  
Isamu Imanishi

1975 ◽  
Author(s):  
B. Binder ◽  
G. Krug ◽  
Th. Vukovich

To obtain a better understanding of the activating mechanism of F XI we studied the interaction of highly purified F XII and F XI with activating agents (kaolin, cephalin) F XII as well as F XI were purified from ACD-plasma (ionic exchange procedures, gel fractionation). Both coagulation factors were obtained with a specific activity per mg protein of approximately 4000 times the value of the original plasma, showing a single band in polyacrylamide gel electrophoresis. The preparations contained less than 1 per cent of their activated forms.F XII and F XI as well as the mixture of both were exposed to kaolin, cephalin, or a kaolin-cephalin mixture, respectively. F XII was adsorbed to about 90 per cent by kaolin alone and the adsorbed fraction was activated completely within minutes; F XI on the other hand was neither adsorbed nor activated by kaolin. The kaolin-activated F XII effected practically no activation of F XI. By cephalin F XII was activated only within hours, but the so activated F XII produced activation of F XI corresponding to F XIIa available in a ratio F XIIa/F XI a of 10/1. A mixture of kaolin and cephalin activated F XII within minutes; ca 20 to 30 per cent of the resulting F XIIa activity became not adsorbed to kaolin and this F XII a activates F XI in the same ratio as in the case of cephalin-activated F XII. Gel fractionation of F XII and F XI together with cephalin revealed that only F XIIa is bound to the phospholipid; no solid complex formation was found between F XI and cephalin or between F XI and F XII.(Supp. by a Grant from the Eisner-Foundation.)


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