Standard

Sravnitel'no-énzimologicheskiǐ analiz kreatinkinaz iz skeletnykh myshts treski, liagushki i krolika. / Petrova, T. A.; Shamova, O. V.; Lyzlova, S. N.

In: Zhurnal Evolyutsionnoi Biokhimii i Fiziologii, Vol. 24, No. 4, 07.1988, p. 489-496.

Research output: Contribution to journal › Article › peer-review

Harvard

Petrova, TA, Shamova, OV & Lyzlova, SN 1988, 'Sravnitel'no-énzimologicheskiǐ analiz kreatinkinaz iz skeletnykh myshts treski, liagushki i krolika.', Zhurnal Evolyutsionnoi Biokhimii i Fiziologii, vol. 24, no. 4, pp. 489-496.

APA

Petrova, T. A., Shamova, O. V., & Lyzlova, S. N. (1988). Sravnitel'no-énzimologicheskiǐ analiz kreatinkinaz iz skeletnykh myshts treski, liagushki i krolika. Zhurnal Evolyutsionnoi Biokhimii i Fiziologii, 24(4), 489-496.

Vancouver

Petrova TA, Shamova OV, Lyzlova SN. Sravnitel'no-énzimologicheskiǐ analiz kreatinkinaz iz skeletnykh myshts treski, liagushki i krolika. Zhurnal Evolyutsionnoi Biokhimii i Fiziologii. 1988 Jul;24(4):489-496.

Author

Petrova, T. A. ; Shamova, O. V. ; Lyzlova, S. N. / Sravnitel'no-énzimologicheskiǐ analiz kreatinkinaz iz skeletnykh myshts treski, liagushki i krolika. In: Zhurnal Evolyutsionnoi Biokhimii i Fiziologii. 1988 ; Vol. 24, No. 4. pp. 489-496.

BibTeX

@article{57c52eedf79c403c93558d137e4b8087,
title = "Sravnitel'no-{\'e}nzimologicheskiǐ analiz kreatinkinaz iz skeletnykh myshts treski, liagushki i krolika.",
abstract = "Electrophoretic studies have been made of the protein composition and isozymic pattern of the creatine kinase from muscles of the cod. It was shown that this enzyme constitutes up to 40% of total water-soluble proteins of muscle tissue. Isolation and purification procedures were suggested for the creatine kinase from cod muscles which allow to obtain the enzyme with the specific activity 250-350 IU/mg. Comparative enzymic analysis of creatine kinases from muscle tissue of the cod, lake frog, and rabbit was also made. Studies were carried out on temperature dependence of the reaction, kinetic constants at temperatures 5 and 30 degrees C were determined together with other physicochemical properties of the enzymes. The revealed species specific differences are discussed in relation to the structure and function of the enzymes in lower vertebrates in vivo.",
author = "Petrova, {T. A.} and Shamova, {O. V.} and Lyzlova, {S. N.}",
year = "1988",
month = jul,
language = "русский",
volume = "24",
pages = "489--496",
journal = "ЖУРНАЛ ЭВОЛЮЦИОННОЙ БИОХИМИИ И ФИЗИОЛОГИИ",
issn = "0044-4529",
publisher = "Издательство {"}Наука{"}",
number = "4",

}

RIS

TY - JOUR

T1 - Sravnitel'no-énzimologicheskiǐ analiz kreatinkinaz iz skeletnykh myshts treski, liagushki i krolika.

AU - Petrova, T. A.

AU - Shamova, O. V.

AU - Lyzlova, S. N.

PY - 1988/7

Y1 - 1988/7

N2 - Electrophoretic studies have been made of the protein composition and isozymic pattern of the creatine kinase from muscles of the cod. It was shown that this enzyme constitutes up to 40% of total water-soluble proteins of muscle tissue. Isolation and purification procedures were suggested for the creatine kinase from cod muscles which allow to obtain the enzyme with the specific activity 250-350 IU/mg. Comparative enzymic analysis of creatine kinases from muscle tissue of the cod, lake frog, and rabbit was also made. Studies were carried out on temperature dependence of the reaction, kinetic constants at temperatures 5 and 30 degrees C were determined together with other physicochemical properties of the enzymes. The revealed species specific differences are discussed in relation to the structure and function of the enzymes in lower vertebrates in vivo.

AB - Electrophoretic studies have been made of the protein composition and isozymic pattern of the creatine kinase from muscles of the cod. It was shown that this enzyme constitutes up to 40% of total water-soluble proteins of muscle tissue. Isolation and purification procedures were suggested for the creatine kinase from cod muscles which allow to obtain the enzyme with the specific activity 250-350 IU/mg. Comparative enzymic analysis of creatine kinases from muscle tissue of the cod, lake frog, and rabbit was also made. Studies were carried out on temperature dependence of the reaction, kinetic constants at temperatures 5 and 30 degrees C were determined together with other physicochemical properties of the enzymes. The revealed species specific differences are discussed in relation to the structure and function of the enzymes in lower vertebrates in vivo.

UR - http://www.scopus.com/inward/record.url?scp=0024046440&partnerID=8YFLogxK

M3 - статья

C2 - 3206952

AN - SCOPUS:0024046440

VL - 24

SP - 489

EP - 496

JO - ЖУРНАЛ ЭВОЛЮЦИОННОЙ БИОХИМИИ И ФИЗИОЛОГИИ

JF - ЖУРНАЛ ЭВОЛЮЦИОННОЙ БИОХИМИИ И ФИЗИОЛОГИИ

SN - 0044-4529

IS - 4

ER -

ID: 11507859