[The immunochemical indices of the structural damage to brain tissue at different periods of traumatic brain disease]. / Immunokhimicheskie pokazateli strukturnogo povrezhdeniia mozgovoi tkani v razlichnye periody travmaticheskoi bolezni golovnogo mozga.

Interorganic and neurospecific liquor proteins were measured in brain injury patients using enzyme immunoassay and radioimmunoassay (maximum sensitivity 2.0 and 0.05-1 ng/ml, respectively). The protein concentrations were found to vary with the time which elapsed since the injury.

[A new highly active proteolytic myelin enzyme and its possible role in the mechanism of the demyelinating process]. / Novyi vysokoaktivnyi proteoliticheskii ferment mielina i ego vozmozhnaia rol' v mekhanizme demieliniziruiushchego protsessa.

The study of the myelin in the rabbit brain and in biological fluids of patients with multiple sclerosis has revealed the presence of a new highly active proteolytic enzyme. The article describes the physicochemical properties of this enzyme. Its role in the pathogenesis of the demyelinizing process is emphasized: normally being coupled with an inhibitor the enzyme is released as a result of the demyelinizing process and becomes active. This leads to the destruction of myelin proteins. Possible factors of enzyme activation are considered. The authors discuss the significance of differences in the activities depending on the stage of the process and the course of multiple sclerosis.

[Isolation and various properties of leucine aminopeptidase from biological fluids of patients with multiple sclerosis]. / Vydelenie i nekotorye svoistva spetsificheskoi leitsinaminopeptidaziz biologicheskikh zhidkostei bol'nykh rasseiannym sklerozom.

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 were detected in blood and cerebrospinal fluid. Estimation of the bound enzyme activity has a diagnostic significance.

[Comparative study of the properties of a proteolytic enzyme isolated from the myelin of animals and from the biological fluids of disseminated sclerosis patients]. / Sravnitel'noe izuchenie nekotorykh svoistv proteoliticheskogo fermenta, vydelennogo iz mielina zhivotnykh i biologicheskikh zhidkostei bol'nykh rasseiannym sklerozom.

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 patients with disseminated sclerosis and then purified. The major part of the enzyme activity in the blood and myelin was bound and was manifested only after special treatment. It is suggested that a similar proteolytic enzyme is present in human myelin, whose activation in demyelinating diseases may result in myelin destruction.