[Effect of one-time and chronic low-intensity irradiation on cathepsin L activity in rat brain].

The effect of the total single and chronic roentgen irradiation in the dose of 0.25 Gy on the rats to alteration dynamics in lysosomal cysteine cathepsin L [CE 3.4.

[Cathepsin L from human brain tumor. Purification and contents].

Cysteine cathepsin L was isolated and purified 1242-fold from human brain. Cathepsin L pH-optimum, Vmax, K(m), lysosomal origin and thiol nature were determined. The distribution of cathepsin L activity in human brain tumours of different histological structure, histogenesis and degree of malignization was studied.

[Organization and development of neurochemical research in the Dnepr area (the 60-80s)].

The development of neurochemical investigations at the Institute of Biochemistry of the National Academy of Sciences of Ukraine initiated by Academician A. V. Palladin, has impelled specialists in some regions of the country to start research in this trend.

[The effect of x-ray radiation and hypoxia on the proteolytic activity of the normal rat spleen and during tumor growth].

The influence of X-radiation on activity of lysosomal enzymes (D, L, H cathepsins) in rat spleen tissue and in inoculated rat sarcoma 45 has been investigated. Intact rats and rats with tumors were subjected to whole-body and sarcoma 45 to local irradiation with doses of 0.155 C/kg and 0.

[Clinico-biological evaluation of the status of newborn infants and the tactics in the management of the early postnatal period].

Biology of the perinatal period as a basis of neonatal management is an area of conceptual controversy. Literature evidence and findings of a clinical and functional study in 175 term newborns support the concept of intrapartum and neonatal stress. This is a rationale for a strategy of maintaining the adaptive mechanisms of the fetus and newborn in a maximal range and active support of neonatal homeostasis.

[Cathepsin H activity in the human brain and human brain neoplasms].

The human brain cathepsin H is shown to be a specific cysteine aminopeptidase with the optimum activity at pH 6.0. Human brain tumours of neuroectodermal (astrocytomas and glioblastomas) and epithelial (meningiomas) origin were used to study the cathepsin H activity in the malignant brain tissue.

[Purification and properties of thiol-activated cathepsin from bovine cerebrum and cerebellum].

Thiol-activated cathepsin was isolated from bovine cerebral hemispheres and cerebellum. The enzyme from the hemispheres was purified by the affinity sorbent chromatography method with the sepharose-4B-immobilized protein substrate, azocasein, and with subsequent separation of nonspecifically sorbed protein by column gel-chromatography on Sephadex G-100. The cathepsin pH-optimum was 6.

[Cathepsin B1 activity in cat brain tissue].

The dependence of the cathepsin B1 (EC 3.4.22.