Biomedical subjects
Publications and source records attributed to Iu V Magerovskiĭ.
A microprocessor analyzer for electrophoregram scanning on cellulose acetate film, agarose and polyacrylamide gels has been designed. The principal characteristics of the device: scanning time 20 seconds, size of the analyzed plate 140 x 110 mm, scanning length 65-85 mm, maximal number of analyzed fractions 10. Analysis and recording of the results takes up to 1 min.
The characteristics of soluble thromboplastin, a new coagulant agent, were under study. This drug is a high-molecular lipoprotein complex of human cadaver brain, purified by gel chromatography. The new preparation has been standardized and compared to thromboplastin preparations manufactured in this country and abroad. Soluble thromboplastin has been found fairly sensitive to reductions of the prothrombin factors levels, it may be used for monitoring the efficacy of indirect anticoagulant therapy, and conforms to WHO regulations for thromboplastin reference agents; this latter fact recommends this new drug as a thromboplastin reference agent in this country.
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It was shown that the cyclic polypeptide antibiotic bacitracin is a competitive inhibitor of fibrinogen clotting by thrombin. Biospecific adsorbents for isolation of thrombin by gramicidin S and bacitracin attachment to silochrome S-80 modified by gamma-glycido-oxypropyl groups were synthesized. The thrombin yield at pH 7.2 and 8.0 was 76.5-96%, purification--6.2-11.6-fold, specific coagulating activity--940-1750 NIH u./mg protein. At pH 6.1 the enzyme does not practically bind to the adsorbents. In all probability, the differences in thrombin binding are due to conformational changes in the enzyme molecule, when pH changes from 6.1 to 7.2. Possible application of the synthesized adsorbents for obtaining laboratory and commercial preparations of thrombin and their perspective use for purification of other blood plasma serine proteinases possessing a narrow specificity are discussed.
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Thrombin purification is conducted by biospecific chromatography on gramicidin C-silochrome C 80. Preparations possessing the fibrinogen-coagulating activity of 2500-3200 NIH units per 1 mg of protein and containing 98% of active sites are obtained. Data obtained from electrophoresis in PAAG with the presence of DS-Na show the alpha-thrombin content to be 96%; the admixture of beta-thrombin possessing no coagulating activity does not exceed 4%. The kinetic constants are presented for thrombin hydrolysis of tosyl-L-arginine methyl ester (TAME), benzoyl-L-arginine ethyl ester (BAEE) and chromogenic substrate S-2238. The addition of isopropanol increases sharply the stability of thrombin when storing it in the aqueous-salt solutions.
Tissue thromboplastin was purified using various chromatographic resins: Sephadex G-200, Ultragel AcA 34, Acrylex P-300 and Toyopearl HW-55F. The purity of the preparations obtained was evaluated by means of the ratio of the thromboplastin solutions absorbency at 540 nm and a protein concentration in the solution expressed as mg/ml. The most purified preparations of tissue thromboplastin were obtained after gel filtration on Toyopearl HW-55F. The thromboplastin preparation produced was used for experimental reproduction of the syndrome of generalized decompensated thrombinogenesis.
The authors compare the effects of Tween-20, Brij-35, Triton X-100 and X-305 on the development of stain for two methods: (1) with phosphoric molybdenic acid forming a complex with malachite blue and (2) with photometry of nonreduced phosphoric molybdenic complex. In the former method the type of detergent affects the degree of absorption of the photo-measured complex and in the latter it affects only the duration of the complex stabilization. Both methods are sufficiently sensitive, rapid, and reproducible. In both cases Triton X-100 was used in routine studies.