Plasma Enzyme Activities1

2015 ◽  
pp. 1-7 ◽  
Author(s):  
J. H. Wilkinson
Keyword(s):  
1968 ◽  
Vol 19 (03/04) ◽  
pp. 438-450
Author(s):  
I. E. T Gan ◽  
B. G Firkin

Summary1. A correlation between platelet aggregation and the plasma enzyme(s) ability to degrade Adenosine Diphosphate (ADP) has been confirmed.2. This plasma activity has been shown to be reduced in 6 patients with uraemia in whom platelet aggregation was demonstrably impaired but not in two whose platelet function was normal. The incorporation of 14C labelled ADP-8-14C was also only reduced in uraemic patients with abnormal platelet aggregation.3. These findings are discussed with particular reference to possible implication in mechanism involved in ADP aggregation of platelets.


1987 ◽  
Vol 21 (1) ◽  
pp. 60-67 ◽  
Author(s):  
C. W. Davy ◽  
P. N. Trennery ◽  
J. G. Edmunds ◽  
J. F. B. Altman ◽  
D. A. Eichler

An investigation of raised plasma aspartate aminotransferase (AST) in marmosets after intramuscular ketamine injection suggested a local myotoxicity. This was confirmed by a range of histopathological findings from myofibrillar striation loss to necrosis. In addition to the elevations in AST levels, creatine kinase and the lactate dehydrogenase-5 isoenzyme levels were elevated. It was further demonstrated that, although the physical properties of the injectable solution (pH, osmolality) and to a lesser extent the injection procedure itself caused slight changes in plasma enzyme levels, the ketamine was predominantly responsible for the lesion. No hepatic interactions were seen. This effect should be taken into consideration when this anaesthetic is used in the marmoset if the primary objectives of the experiment entail routine blood analyses.


1972 ◽  
Vol 30 (4) ◽  
pp. 302-308
Author(s):  
David A. Cunningham ◽  
Jerry B. Critz

2002 ◽  
Vol 57 (7) ◽  
pp. 1907-1916 ◽  
Author(s):  
M. Aksoy ◽  
A. Kaya ◽  
H. Vatansev ◽  
T. Tekeli

Blood ◽  
1986 ◽  
Vol 68 (3) ◽  
pp. 640-645 ◽  
Author(s):  
K Takahashi ◽  
HJ Cohen

Selenium-deficient humans and animals are known to be deficient in glutathione peroxidase (GSHPx) activity in their cells and plasma. To determine the relationship between enzyme activity and protein content, the enzyme was purified from human erythrocytes, and polyclonal antibodies were made against the purified protein in rabbits. These antibodies were found to be monospecific, noninhibitory, and capable of precipitating the enzymatic activity. All the GSHPx activity in erythrocytes and almost all the activity in neutrophils and platelets was precipitated by these antibodies. None of the plasma enzyme was precipitated by these antibodies, indicating that the plasma enzyme activity was attributable to a different selenium dependent protein moiety. Utilizing a radioimmunoassay, we were able to determine that there was a direct relationship between GSHPx activity and protein content in the erythrocytes of both normal and selenium-deficient individuals, and a similar relationship between control and selenium- deficient rat erythrocytes and liver cells. Thus, the ability to examine GSHPx as a protein resulted in two new observations concerning the selenium-dependent GSHPx. The first is that the plasma enzyme is antigenically distinct from the erythrocyte enzyme, and the second is that in the absence of selenium, there is a concomitant decrease in GSHPx protein.


2021 ◽  
Vol 10 (1) ◽  
pp. 631-634
Author(s):  
Pradeep Kumar Godwal ◽  
Vijay Kumar ◽  
Meenaxi Sareen ◽  
Hakim Manzer ◽  
Anil Moolchandani ◽  
...  

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