T. S. Baskaeva

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Specific form of leucine aminopeptidase (which was distinct from other forms of the enzyme found in blood) was characterized by its physico-chemical properties--pH optimum, substrate specificity, electrophoretic mobility and molecular mass. The enzyme was isolated from biological fluids of patients with multiple sclerosis. Free and bound forms of the enzyme(More)
The problem of the metabolic inertia of myelin is now being reexamined [7]. A number of enzymes which evidently play a direct part in metabolism of the structural components of the biological membrane have been found in myelin taken from the central nervous system (CNS) [5]~ The presence of at least two proteolytic enzymes has been demonstrated in myelin(More)
A proteolytic enzyme with the activity of 8-26 U/mg protein was isolated from purified animal myelin preparation obtained by an original technique. The optimal pH of the enzyme was found to be 9.6-9.8. Its substrate specificity was studied. An enzyme with similar characteristics and identical electrophoretic mobility was isolated from the blood serum of(More)
Mitochondrial monoamine oxidase (MAO) activity in various parts of the brain (cerebral hemispheres, brain stem, cerebellum) was studied in experiments on rabbits in the normal state and 1.5 h and 1 and 5 days after closed head injury. Serotonin creatininesulfate was used as the substrate. Acute closed head injury was shown to cause a sharp decrease in MAO(More)
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