Українська English

ISSN 2522-9028 (Print)
ISSN 2522-9036 (Online)
DOI: https://doi.org/10.15407/fz

Fiziologichnyi Zhurnal

is a scientific journal issued by the

Bogomoletz Institute of Physiology
National Academy of Sciences of Ukraine

Editor-in-chief: V.F. Sagach

The journal was founded in 1955 as
1955 – 1977 "Fiziolohichnyi zhurnal" (ISSN 0015 – 3311)
1978 – 1993 "Fiziologicheskii zhurnal" (ISSN 0201 – 8489)
1994 – 2016 "Fiziolohichnyi zhurnal" (ISSN 0201 – 8489)
2017 – "Fiziolohichnyi zhurnal" (ISSN 2522-9028)

Fiziol. Zh. 2005; 51(5): 85-89

Ratio of low- and high spincytochrome p-450 in microsomesof ndea -induced hepatomas

O.R. Melnikov, V.Ya.Momot,T.V. Pyatchanina, E.P.Sidorik.

    R.E.Kavetsky Institute of Experimental Pathology, Oncologyand Radiobiology, National Academy of Sciences of Ukraine, Kyiv



Abstract

Content of high- and low-spin oxidized CYP was determined in liver microsomes and NDEA-induced hepatomas by method of optic spectrofotometry. Value of spin states ratio in hepatoma was shown to be greater then in liver. It in- creased under the action of inductors, which caused the syn- thesis of isoforms in high-spin configuration. Data obtained as a result of investigation of CYP isoform composition and metabolite phenotype of hepatoma have suggested that shift in balance of spin states in hepatoma was due to the decrease in the quantities of IIC11 and IIE1 isoforms as well as to the high level of IA1 isoform expression.

Full text: (PDF, in Ukrainian)

References

  1. Герасимов К.Е., Гуляева Л.Ф., Мишин В.М., ЦырловИ.Б. Множественные формы цитохрома Р-450.Характеристика изолированной амидопирин-N-деметилазы // Биохимия. – 1988. – 53, №1. – С. 3–10.
  2. Де Пьер Ж., Дальнер Г. Выделение, субфракцио-нирование и характеристика эндоплазматическойсети. – В кн.: Биохимическое исследование мембран. –М.: Наука, 1979. – С. 76–123.
  3. Кобляков В.А. Цитохром Р-450 в опухолях и впроцессе канцерогенеза // Биохимия. – 1995. – 60,№11. – С. 1043–1058.
  4. Мельников О.Р., Момот В.Я., Пятчанина Т.В.,Сидорик Е.П. Изменение соотношения ферро- иферрицитохрома Р-450 в печени животных какусловие трансформации гепатоцитов под действиемN-нитрозодиэтиламина // Эксперим. онкология. –2000. – 22, №3. – С. 141–143.
  5. Davydov R., Makris T.M., Kofman V. Hydroxylationof camphor by reduced oxy-cytochrome P450cam:mechanistic implications of EPR and ENDOR studiesof catalytic intermediates in native and mutantenzymes // J. Amer. Chem. Soc. – 2001. – 123, №7. –P. 1403–1415.
  6. Dorsey T., McDonald P.W., Roels O.A. A heated bi-uret - Folin protein assay which gives equal absor-bance with different proteins //Anal. Biochem. – 1977. –78. – P. 156–164.
  7. Jefcoate C.R.E., Calabrese R.L., Gatlor J.I. The use ofn-oktylamine and ethyl isocyanide difference spectros-copy in the quantitative determination of high- andlow- spin P-450 // Mol. Pharmacol. – 1970. – №6. –P. 391–401.
  8. Laemmly U.K. Cleavance of structural proteins duringthe assembly of head of bacteriophage T4 // Nature. –1970. – 237. – P. 680– 685.
  9. 9. Lange R., Duclous N., Perin F. Particular cytochromeP-450-dependent steroid metabolism: A new class ofmouse liver tumor markers // Carcinogenesis. – 1989. –10, №5. – P. 1871–1877.
  10. 10. Omura T., Sato R. The carbon monooxide-binding pig-ment of liver microsomes // J.Biol. Chem. – 1964. –239, №7. – P. 2370–2378.
  11. Sakai H., Park S.S., Kikkava Y. Differential oxidaseactivity of hepatic and pulmonary microsomal cyto-chrome P-450 isozymes after treatment with cyto-chrome P-450 inducers //Biochim. and Biophys.Res.Commun. – 1992. – 187, № 3. – P. 1262–1269.
  12. Wiebel F.J., Park S.S, Kiefer F.,Gelboin H.V. Analysisby monoclonal antibodies specific for cytochrome P-450 from rat liver induced by 3-methylcholanthrene orphenobarbital //
© National Academy of Sciences of Ukraine, Bogomoletz Institute of Physiology, 2014-2024.