Biochemical and Physiological Approaches to Species Specificity in Herbicide Science

1975 ◽  
Vol 20 (2) ◽  
pp. 49-54
Author(s):  
Kozo ISHIZUKA
Keyword(s):  
1968 ◽  
Vol 20 (03/04) ◽  
pp. 457-464 ◽  
Author(s):  
L Gonyea ◽  
R Herdman ◽  
R. A Bridges

SummaryAn anticoagulant occurring in 4 of 6 patients with SLE has been demonstrated by a sensitive assay utilizing an ammonium sulfate fraction of serum. The anticoagulant functions as an inhibitor of the activation of prothrombin. No species specificity was demonstrable. The inhibitor behaves clinically and chromatographically as an immunoglobulin, although an attempt to demonstrate directly the antibody nature of the inhibitor was not successful.A severe, apparently independent, decrease in the level of prothrombin was observed in the patient with hemorrhagic symptoms. In contrast to the anticoagulant activity, the low prothrombin has persisted during treatment.


2010 ◽  
Vol 18 (1) ◽  
pp. 1 ◽  
Author(s):  
Chen Yan ◽  
Li Hongqing ◽  
Liu Min ◽  
Chen Xiaoyong
Keyword(s):  

2010 ◽  
Vol 79 (2) ◽  
pp. 401-409 ◽  
Author(s):  
Michael G. Anderson ◽  
Dianne H. Brunton ◽  
Mark E. Hauber

Virology ◽  
2006 ◽  
Vol 347 (2) ◽  
pp. 410-421 ◽  
Author(s):  
Noah Butler ◽  
Lecia Pewe ◽  
Kathryn Trandem ◽  
Stanley Perlman

1989 ◽  
Vol 40 (3) ◽  
pp. 673-680 ◽  
Author(s):  
Albert B. Reynolds ◽  
Ted S. Thomas ◽  
Wendy L. Wilson ◽  
Gene Oliphant

1940 ◽  
Vol 71 (5) ◽  
pp. 585-590 ◽  
Author(s):  
E. E. Ecker ◽  
L. Pillemer

Oxidized and reduced proteins were prepared from the ocular lenses of sheep, swine, chicken and fish (pike). The proteins were prepared under conditions designed to avoid denaturation and to produce relatively pure compounds. Serologic studies revealed that species specificity is demonstrable in the proteins from chicken and fish lenses, but in the more closely related species (swine and sheep) this characteristic is not so evident. Serologic differences may be detected in the lens preparations from a single species, depending on the redox state of the protein.


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