ChemInform Abstract: BIOLOGICALLY ACTIVE STABLE RADICALS; VII. SPIN LABELING OF NUCLEOSIDES AND NUCLEOTIDES AT THE AMINO GROUP

1979 ◽  
Vol 10 (31) ◽  
Author(s):  
R. I. ZHDANOV ◽  
V. A. POROTIKOVA ◽  
E. G. ROZANTSEV
Synthesis ◽  
1979 ◽  
Vol 1979 (04) ◽  
pp. 267-269 ◽  
Author(s):  
R. I. Zhdanov ◽  
V. A. Porotikova ◽  
E. G. Rozantsev

Synthesis ◽  
1977 ◽  
Vol 1977 (05) ◽  
pp. 312-313 ◽  
Author(s):  
R. I. ZHDANOV ◽  
N. G. KAPITANOVA ◽  
E. G. ROZANTSEV

2013 ◽  
Vol 60 (1) ◽  
Author(s):  
Anna Dąbrowska ◽  
Marek Szołtysik ◽  
Konrad Babij ◽  
Marta Pokora ◽  
Aleksandra Zambrowicz ◽  
...  

The main objective of this study was to determine potential application of a serine proteinase derived from Asian pumpkin for obtaining biologically active peptides from casein. The course of casein hydrolysis by three doses of the enzyme (50, 150, 300 U/mg of protein) was monitored for 24 hours by the determinations of: hydrolysis degree DH (%), free amino group content (μmole Gly/g), RP HPLC peptide profiles and by polyacrylamide gel electrophoresis. In all hydrolyzates analyzed antioxidant activities were determined using three tests: the ability to reduce iron ions in FRAP test, the ability to scavenge free radicals in DPPH test, and Fe(2+) chelating activity. The antimicrobial activity of obtained peptide fractions was determined as the ability to inhibit the growth of Escherichia coli, Bacillus cereus and Pseudomonas fluorescens in a diffusion plate test. The deepest degradation, expressed as the DH [%] and the free amino group content (67% and 7528 µmole Gly/mg, respectively), was noted in samples hydrolyzed with 300 U/ml of enzyme for 24 hours, while in other samples the determined values were about three and two times lower. The results were in agreement with the peptide profiles obtained by RP HPLC. The highest antioxidative activities determined in all tests were seen for the casein hydrolysate obtained with 300 U/mg protein of serine proteinase after 24 h of reaction (2.15 µM Trolox/mg, 96.15 µg Fe(3+)/mg, 814.97 µg Fe(2+)/mg). Antimicrobial activity was presented in three preparations. In other samples no antimicrobial activity was detected.


1979 ◽  
Vol 23 (2) ◽  
pp. 155-162 ◽  
Author(s):  
V.A. Sukhanov ◽  
R.I. Zhdanov ◽  
V.I. Shvets

1977 ◽  
Vol 165 (1) ◽  
pp. 43-47 ◽  
Author(s):  
C R Snell ◽  
D G Smyth

[8-Lysine]oxytocin was synthesized on a solid support and possessed an oxytocic activity of 100 +/- 6 units mumol on the isolated rat uterus. The epsilon-carbamoyl, epsilon-3-carboxypropionyl and epsilon-3-carboxybutryl derivatives were prepared and had uterotonic activities of 400, 55 and 50 units/mumol respectively. [8-Lysine]oxytocin was coupled unambiguously through the epsilon-amino group to the carboxyl groups of carboxymethylated dextrans or epsilon-3-carboxypropionly-gelatin. The macromolecular oxytocins were water-soluble and retained signigicant oxytocic activity. [8-Lysine]oxytocin should prove a useful ligand for affinity chromatography of oxytocin-binding proteins.


1985 ◽  
Vol 28 (9) ◽  
pp. 1371-1375 ◽  
Author(s):  
Thomas R. Herrin ◽  
Alford M. Thomas ◽  
Thomas J. Perun ◽  
James C. Mao ◽  
Stephen W. Fesik

Author(s):  
B. V. Rozynov ◽  
R. I. Zhdanov ◽  
O. S. Reshetova ◽  
N. G. Kapitanova ◽  
Z. L. Gordon ◽  
...  

Author(s):  
R. I. Zhdanov ◽  
N. G. Kapitanova ◽  
�. G. Rozantsev

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