Wyniki wyszukiwania - Biblioteka Nauki

1

Aktynomycyny i ich antymetaboliczne działanie

100%

Galasinski W.

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tom 12

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nr 1

2

Biosynteza kolagenu

84%

Bankowski E. , Galasinski W.

|

nr 4

3

Isolation and characterization of elongation factor EF-2 from Guerin tumour

67%

Jablonowska K. , Kopacz-jodczyk T. , Niedzwiedzka J. , Galasinski W.

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nr 3-4

4

The effect of phosphorylation of the EF-2 isolated from rat liver cells on protein biosynthesis in vitro

67%

Gajko A. , Sredzinska K. , Marcinkiewicz C. , Galasinski W.

Acta Biochimica Polonica

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1991

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tom 38

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nr 3

5

Purification and properties of the heterogeneous subunits of elongation factor EF-1 from Guerin epithelioma cells

67%

Marcinkiewicz C. , Gajko A. , Galasinski W.

Acta Biochimica Polonica

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1991

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tom 38

|

nr 1

6

Differences in the structures of the elongation factors (EF-2) isolated from guerin epithelioma and rat liver

67%

Sredzinska K. , Gajko A. , Galasinski W.

|

1991

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tom 39

|

nr 2

7

The phosphorylation of elongation factor EF-1 isolated from guerin epithelioma

67%

Marcinkiewicz C. , Gajko A. , Galasinski W.

Acta Biochimica Polonica

|

1992

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tom 39

|

nr 1

8

EF-1alpha is a target site for inhibitory effect of quercetin in the peptide elongation process

67%

Marcinkiewicz C. , Galasinski W. , Gindzienski A.

Acta Biochimica Polonica

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1995

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tom 42

|

nr 3

EN

The effect of quercetin (3,3',4',5,7-pentahydroxyflavone) on the polypeptide elongation system isolated from rat liver cells, was investigated. Quercetin inhibited [ 4C]leucine incorporation into proteins in vitro and the inhibitory effect is being directed towards the elongation factor eEF-1, but not to eEF-2 and ribosomes. Quercetin was found to form a complex with EF-la, which was inactive in GTP-dependent binding to ribosomes. It can be suggested that quercetin can block the total or the part of the domain of EF-la structure that is responsible for formation of the ternary complex EF-la-GTP-i14C]Phe-tRNA and therefore preventing formation of the quaternary complex with ribosomes.

9

Purification and characterization of the protein kinase eEF-2 isolated from rat liver cells

67%

Gajko A. , Galasinski W. , Gindzienski A.

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1994

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tom 41

|

nr 4

XX

The elongation factor 2 (eEF-2) protein kinase was isolated from rat liver cells, purified and partly characterized. It was found that the enzyme exists in an inactive form in the homogenate of rat liver. The active fraction of kinase eEF-2 was obtained after removal of the inhibitory substance by hydroxyapatite column chromatography. The purified enzyme is an electTophoretically homogeneous protein with relative molecular mass of approximately 90000 and isoelectric point, pi = 5.9. The enzyme specifically phosphorylates the elongation factor eEF-2 in the presence of calmodulin and Ca2+.

10

Badania nad kwasami nukleinowymi drożdży

67%

Galasinski W.

Postępy Biochemii

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1965

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tom 11

|

nr 1

11

Further studies on the quaternary structure of yeast casein kinase II

59%

Szyszka R. , Lopaczynski W. , Galasinski W. , Grankowski N. , Gasior E.

Acta Biochimica Polonica

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1986

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tom 33

|

nr 1

12

Sprawozdanie. IX Zjazd Federacji Europejskich Towarzystw Biochemicznych (FEBS). Budapeszt, 25-30 sierpień 1974

30%

Duszynski J. , Fikus M. , Galasinski W. , Gasior E. , Grabczewska E. , Kochman M. , Kopec M. , Paszewski A. , Pilarska M. , Potempska A. , Romanowska E. , Rossowski W. , Stzrelecka-Golaszewska H. , Szewczuk A. , Wolajtys E. , Zborowski J. , Zielinska Z.

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nr 2