Issledovanie vzaimodeǐstviia spinovykh metok i zondov s Na+,K+-ATPazoǐ.

A. V. Kulikov; F. T. Umarova; G. I. Likhtenshteǐn

Issledovanie vzaimodeǐstviia spinovykh metok i zondov s Na+,K+-ATPazoǐ.

Translated title of the contribution: Interaction of spin labels and probes with Na+,K+-ATPase

A. V. Kulikov, F. T. Umarova, G. I. Likhtenshteǐn

Department of Chemistry

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

Abstract

Localization of the PCMB-R spin label and benzocarboline probe bound with the purified preparation of pig kidney-Na+, K(+)-ATPase relative to active site of the enzyme was studied by EPR method. The number of Mn2+ ions in active site of the enzyme as well as that bound with lipids was determined from EPR spectra of paramagnetic manganese ions replacing magnesium ions were measured in frozen protein samples of Na2+, K(+)-ATPase at 77 K. It has been found that sulfhydryl group of the enzyme modified by PCMB-R and benzocarboline probe are placed at distances 38 A and 50 A, respectively, from Mn2+ ions in the active site of Na+, K(+)-ATPase. Evaluation of the immersion depth of the nitroxyl radical into protein globule showed that benzocarboline probe was immobilized near the macromolecular protein surface; there are two bound probe sites, distinguished by accessibility of ferricyanide ions.

Translated title of the contribution	Interaction of spin labels and probes with Na+,K+-ATPase
Original language	Russian
Pages (from-to)	38-45
Number of pages	8
Journal	Ukrainian Biochemical Journal
Volume	65
Issue number	3
State	Published - 1 May 1993

ASJC Scopus subject areas

Biochemistry

Cite this

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title = "Issledovanie vzaimodeǐstviia spinovykh metok i zondov s Na+,K+-ATPazoǐ.",

abstract = "Localization of the PCMB-R spin label and benzocarboline probe bound with the purified preparation of pig kidney-Na+, K(+)-ATPase relative to active site of the enzyme was studied by EPR method. The number of Mn2+ ions in active site of the enzyme as well as that bound with lipids was determined from EPR spectra of paramagnetic manganese ions replacing magnesium ions were measured in frozen protein samples of Na2+, K(+)-ATPase at 77 K. It has been found that sulfhydryl group of the enzyme modified by PCMB-R and benzocarboline probe are placed at distances 38 A and 50 A, respectively, from Mn2+ ions in the active site of Na+, K(+)-ATPase. Evaluation of the immersion depth of the nitroxyl radical into protein globule showed that benzocarboline probe was immobilized near the macromolecular protein surface; there are two bound probe sites, distinguished by accessibility of ferricyanide ions.",

author = "Kulikov, {A. V.} and Umarova, {F. T.} and Likhtenshteǐn, {G. I.}",

year = "1993",

month = may,

day = "1",

language = "רוסית",

volume = "65",

pages = "38--45",

journal = "Ukrainian Biochemical Journal",

issn = "0201-8470",

publisher = "Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine (NASU)",

number = "3",

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TY - JOUR

T1 - Issledovanie vzaimodeǐstviia spinovykh metok i zondov s Na+,K+-ATPazoǐ.

AU - Kulikov, A. V.

AU - Umarova, F. T.

AU - Likhtenshteǐn, G. I.

PY - 1993/5/1

Y1 - 1993/5/1

N2 - Localization of the PCMB-R spin label and benzocarboline probe bound with the purified preparation of pig kidney-Na+, K(+)-ATPase relative to active site of the enzyme was studied by EPR method. The number of Mn2+ ions in active site of the enzyme as well as that bound with lipids was determined from EPR spectra of paramagnetic manganese ions replacing magnesium ions were measured in frozen protein samples of Na2+, K(+)-ATPase at 77 K. It has been found that sulfhydryl group of the enzyme modified by PCMB-R and benzocarboline probe are placed at distances 38 A and 50 A, respectively, from Mn2+ ions in the active site of Na+, K(+)-ATPase. Evaluation of the immersion depth of the nitroxyl radical into protein globule showed that benzocarboline probe was immobilized near the macromolecular protein surface; there are two bound probe sites, distinguished by accessibility of ferricyanide ions.

AB - Localization of the PCMB-R spin label and benzocarboline probe bound with the purified preparation of pig kidney-Na+, K(+)-ATPase relative to active site of the enzyme was studied by EPR method. The number of Mn2+ ions in active site of the enzyme as well as that bound with lipids was determined from EPR spectra of paramagnetic manganese ions replacing magnesium ions were measured in frozen protein samples of Na2+, K(+)-ATPase at 77 K. It has been found that sulfhydryl group of the enzyme modified by PCMB-R and benzocarboline probe are placed at distances 38 A and 50 A, respectively, from Mn2+ ions in the active site of Na+, K(+)-ATPase. Evaluation of the immersion depth of the nitroxyl radical into protein globule showed that benzocarboline probe was immobilized near the macromolecular protein surface; there are two bound probe sites, distinguished by accessibility of ferricyanide ions.

UR - http://www.scopus.com/inward/record.url?scp=18344419269&partnerID=8YFLogxK

M3 - מאמר

AN - SCOPUS:18344419269

SN - 0201-8470

VL - 65

SP - 38

EP - 45

JO - Ukrainian Biochemical Journal

JF - Ukrainian Biochemical Journal

IS - 3

ER -

Issledovanie vzaimodeǐstviia spinovykh metok i zondov s Na+,K+-ATPazoǐ.

Abstract

ASJC Scopus subject areas

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