Wyniki wyszukiwania

1

Aktynomycyny i ich antymetaboliczne działanie

100%

Galasinski W.

Postępy Biochemii

|

1966

|

tom 12

|

nr 1

2

Biosynteza kolagenu

84%

Bankowski E., Galasinski W.

Postępy Biochemii

|

1974

|

tom 20

|

nr 4

3

Tkankowe enzymy kolagenolityczne

84%

Bankowski E., Galasinski W.

Postępy Biochemii

|

1970

|

tom 16

|

nr 1

4

Isolation and properties of the subunit form EF-1C of elongation factor 1 from Guerin epithelioma cells

84%

Marcinkiewicz C., Galasinski W.

Acta Biochimica Polonica

|

1993

|

tom 40

|

nr 2

EF-1C is a component of the aggregate EF-1B, consisting of the subunit forms EF-1A-EF-1C; it was isolated by dissociation of this aggregate in the presence of GTF. The subunit form EF-1C stimulates binding of aminoacyl-tRNA to ribosomes, catalysed by EF-1A, similarly as EF-lßy which stimulates the activity of EF-1 in other eukaryotic cells. EF-1C in the presence of 6 M urea was separated into two polypeptides. Polypeptide of molecular mass 32000 Da is responsible for regeneration of the EF-1A-GTP active complex. Thermal sensitivity of EF-1A was much higher than that of EF-1B, thus a protective role of EF-1C in the EF-1AEF-1C complex is suggested.

5

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

68%

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

Acta Biochimica Polonica

|

1983

|

tom 30

|

nr 3-4

6

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

68%

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

Acta Biochimica Polonica

|

1991

|

tom 38

|

nr 3

7

Isolation, purification and chemical composition of insoluble collagen from guerin epithelioma

68%

Bankowski E., Galasinski W., Gindzienski A., Rzeczycki W.

Acta Biochimica Polonica

|

1975

|

tom 22

|

nr 3

8

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

68%

Marcinkiewicz C., Gajko A., Galasinski W.

Acta Biochimica Polonica

|

1991

|

tom 38

|

nr 1

9

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

68%

Sredzinska K., Gajko A., Galasinski W.

Bulletin of the Polish Academy of Sciences. Biological Sciences

|

1991

|

tom 39

|

nr 2

10

Purification and properties of catalase from Mycobacterium smegmatis

68%

Galasinski W., Wolosowicz N., Tysarowski W.

Acta Biochimica Polonica

|

1962

|

tom 09

|

nr 3

11

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

68%

Marcinkiewicz C., Galasinski W., Gindzienski A.

Acta Biochimica Polonica

|

1995

|

tom 42

|

nr 3

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.

12

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

68%

Gajko A., Galasinski W., Gindzienski A.

Acta Biochimica Polonica

|

1994

|

tom 41

|

nr 4

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+.

13

The participation of ribosomes in protein glycosylation. Interaction of the ribosome-UDP-N-acetyl-glucosamine complex with dolichol phosphate

68%

Paszkiewicz-Gadek A., Porowska H., Galasinski W.

Acta Biochimica Polonica

|

1992

|

tom 39

|

nr 3

UDP-N-acetylglucosaminc can be bound by pure ribosomes. The part of N-acetylglucosamine-1-P can be transferred from the complex ribosome-UDP-N-acetylglucosamine onto dolichol phosphate. Evidence Is presented that N-acetylglucosamine bound to dolichol phosphate can be transferred to the nascent peptide synthesized on the ribosomc.

14

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

68%

Marcinkiewicz C., Gajko A., Galasinski W.

Acta Biochimica Polonica

|

1992

|

tom 39

|

nr 1

15

Badania nad kwasami nukleinowymi drożdży

67%

Galasinski W.

Postępy Biochemii

|

1965

|

tom 11

|

nr 1

16

Further studies on the quaternary structure of yeast casein kinase II

60%

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

Acta Biochimica Polonica

|

1986

|

tom 33

|

nr 1

17

Elongation factors from the Guerin epithelioma and rat liver cells

60%

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

Acta Biochimica Polonica

|

1993

|

tom 40

|

nr 4

18

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

31%

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.

Postępy Biochemii

|

1975

|

tom 21

|

nr 2

Ograniczanie wyników

Aktynomycyny i ich antymetaboliczne działanie

Biosynteza kolagenu

Tkankowe enzymy kolagenolityczne

Isolation and properties of the subunit form EF-1C of elongation factor 1 from Guerin epithelioma cells

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

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

Isolation, purification and chemical composition of insoluble collagen from guerin epithelioma

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

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

Purification and properties of catalase from Mycobacterium smegmatis

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

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

The participation of ribosomes in protein glycosylation. Interaction of the ribosome-UDP-N-acetyl-glucosamine complex with dolichol phosphate

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

Badania nad kwasami nukleinowymi drożdży

Further studies on the quaternary structure of yeast casein kinase II

Elongation factors from the Guerin epithelioma and rat liver cells

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