I. A. Surova

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The pharmacokinetics of total platinum (Pt) were investigated after a single oral dose of (OC-6-43-bis(acetato)(1-adamantylamine)amminedichloroplatinum (IV) (LA-12). A dose of 3 mg/kg (n = 3) and 30 mg/kg (n = 3) was given to two parallel groups of pigs (n = three each). Pt was measured in the blood, urine and feces by atomic absorption spectrometry. Blood(More)
Interspecies differences in glycosidation potential in mammalian tissues represent a factor contributing to ambiguity when endobiotic and/or xenobiotic metabolic pathways are extrapolated from animals to man. Using the TLC/autoradiographic technique, we conducted an in vitro investigation involving mouse, rat, monkey, as well as human liver and kidney(More)
Glu,Asp-specified protease hydrolysate of intracellular serine proteinase (ISP) was separated by ion-exchange chromatography on a sulphocationite resin followed by HPLC to yield 30 individual peptides. Their sequences, spanning to 243 amino acid residues, were determined by the manual Edman procedure. Four overlapping fragments were reconstructed by(More)
Three proteolytic enzymes-the metalloproteinase, SFMP, and two serine proteinases, SFSP and SFTP-have been isolated and purified from the culture fluid of Streptomyces fradiae using chromatography on bacitracin-silochrome, bacitracin-Sepharose, DEAE-cellulose and fractionation by ammonium sulfate. Study of physico-chemical and functional properties of the(More)
Chymotrypsin hydrolyzate of the intracellular serine protease was separated by ion-exchange chromatography on a sulphocationite resin followed by HPLC to yield fifty one individual peptides. Their sequences, corresponding in total to 381 amino acid residues, were determined by the manual Edman procedure.
The structure of B-5 fragment obtained under degradation of pig pepsin by cyanogen bromide is determined. B-5 fragment is a central part of pepsin molecule and it contains 46 amino acids, including a functionally important aspartic residue of the active site of the enzyme. Amino acid sequence of B-5 fragment was established by means of sequenator analysis(More)
The automatic Edman procedure was applied to elucidate N-terminal sequences of swine pepsinogen, pepsin, and the fragments of its degradation by BrCN, i. e. B-1 and B-5. A "Beckman" model 890 instrument was used in experiments. 50 amino acid residues were split off the pepsinogen molecule and identified and 55 amino acid residues-off the pepsin molecule by(More)
By hydrating this furocoumarin with oxalic acid we obtained its hydrate C1d-t!GO6, mp 114-115°C (alcohol), and by isomerizing it with 10% sulfuric acid we obtained a substance of the composition Ctd-t1405, mp 132-184 ° C. All the properties of the substance with mp 105--106 ° C and of the products of its hydration and isomerization agreed with the(More)
Method of isolation of intracellular serine protease was modified. Gramicidin S-sepharose CL-4B with a higher content of the ligand, synthesized through a modified procedure, was used as an affinity sorbent which simplified the purification and led to the pure enzyme with high specific activity and 90% yield. Trypsin hydrolyzate of the protease was(More)
The pept ide B-5 formed in the c leavage of reduced ca rboxymethy la ted porc ine pepsin cons i s t s of 40-43 amino acid r e s idues . A c h a r a c t e r i s t i c fea ture of it is the compara t ive ly high content of hydrophi l ic amino acids. P rev ious ly , by the s tepwise spl i t t ing off of methyl thiohydantoins the following N t e r m i n a l(More)