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[Structure-activity significance of the N-terminal segment of the alpha-subunit of gonadotropin of the Russian sturgeon]. / Strukturno-funktsional'noe znachenie N-kontsevogo uchastka alpha- sub''edinitsy gonadotropina russkogo osetra.

Zenkevich, G A; Kirstukas, I P; Latse, Z M; Slanke, V P; Val'dman, A R.

Dokl Akad Nauk SSSR ; 308(6): 1494-6, 1989.

Article in Russian | MEDLINE | ID: mdl-2482161

Subject(s)

Fishes/metabolism , Glycoprotein Hormones, alpha Subunit/metabolism , Amino Acids/analysis , Animals , Macromolecular Substances , Structure-Activity Relationship

[Structural-functional role of imidazole groups of gonadotropin in the Russian sturgeon]. / Strukturno-funktsional'noe znachenie imidazol'nykh grupp gonadotropina russkogo osetra.

Zenkevich, G A; Kirstukas, I P; Latse, Z M; Slanke, V P; Val'dman, A R.

Dokl Akad Nauk SSSR ; 296(3): 755-7, 1987.

Article in Russian | MEDLINE | ID: mdl-3691313

Subject(s)

Fishes/metabolism , Gonadotropins/analysis , Imidazoles/analysis , Animals , Histidine/analysis , Protein Conformation

[Properties of subunits as components of the antigenic structure of gonadotropin of the Russian sturgeon]. / Svoistva sub''edinits kak komponentov antigennoi struktury gonadotropina russkogo osetra.

Zenkevich, G A; Slanke, V P; Latse, Z M; Kirstukas, I P; Val'dman, A R.

Dokl Akad Nauk SSSR ; 297(6): 1480-2, 1987.

Article in Russian | MEDLINE | ID: mdl-2452062

Subject(s)

Epitopes/analysis , Fishes/metabolism , Gonadotropins/immunology , Animals , Fishes/immunology , Gonadotropins/analysis , Immunodiffusion , Protein Conformation

[Quantitative determination of L-asparaginase and L-asparagine on the apparatus "Ferment-1"]. / Kolichestvennoe opredelenie L-asparaginazy i L-asparagina na pribore "Frement-1"

Zhagat, R A; Buka, M R; Kirstukas, I P.

Lab Delo ; (2): 89-92, 1977.

Article in Russian | MEDLINE | ID: mdl-68151

Subject(s)

Asparaginase/analysis , Asparagine/analysis , Conductometry/instrumentation , Humans

[Determination of the transferase activity of L-asparaginase]. / Opredelenie transferaznoi aktivnosti L-asparaginazy

Buka, M R; Zhagat, R A; Kirstukas, I P; Chepuka, L Y.

Vopr Med Khim ; 21(5): 548-52, 1975.

Article in Russian | MEDLINE | ID: mdl-3024

ABSTRACT

A method for determination of the transferase activity of 1-asparaginase in presence of hydroxylamine is developed. The optimally determined quantity of the enzyme was from 0.7 to 20 i. u. The conditions optimal for the enzymatic reaction and for quantitative estimation of 1-aspartyl-beta-hydroxamic acid were studied. The transferase and hydrolase activities of 1-asparaginase from E. coli were compared. The enzyme catalyzed at equal rates hydrolysis and hydroxylaminolysis of 1-asparagine.

Subject(s)

Asparaginase/metabolism , Transferases/metabolism , Escherichia coli/enzymology , Hydrogen-Ion Concentration , Hydroxylamines/pharmacology , Kinetics

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