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

100%

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.

Nonidentity of subunits of human kidney arginase A1 and human liver arginase A5

63%

Porembska Z., Grabon W., Zelazowska E., Czeczot H., Zamecka E.

Acta Biochimica Polonica

1993

tom 40

nr 4

The main forms of arginase Ai from human kidney and As from human liver were purified to homogeneity. Molecular weight of both forms of enzyme approximates 120000. In the presence of EDTA these arginases dissociate into single type distinct subunits. Mr of both kinds of subunits is 30000. Similarly as native arginase forms, they differ in electric charge and display complete immunological incompatibility.

Ograniczanie wyników

2 Acta Biochimica Polonica

1 Czeczot H.

1 Galasinski W.

1 Grabon W.

1 Marcinkiewicz C.

1 Porembska Z.

1 Zamecka E.

1 Zelazowska E.

2 1993

Wyniki wyszukiwania

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

Nonidentity of subunits of human kidney arginase A1 and human liver arginase A5