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001-es BibID:	BIBFORM045685
Első szerző:	Góth László (analitikus)
Cím:	Human erythrocyte catalase, isolation with an improved method, characterization and comparison to bovine liver catalase / Goth L.
Dátum:	1989
Megjegyzések:	Catalase enzyme was purified from human erythrocytes. The modified procedure of Mörikofer-Zwez et. al. [Eur. J. Biochem. 11: 49-57, 1969] yielded erythrocyte catalase with high specific activity and with one band on SDS polyacrylamide gel. Its other characteristics (isoelectric point; E405/280, E1%1cm at 280 nm and 405 nm) were in agreement with previously described findings. The results obtained for molecular mass, electrophoretic mobility, chromatographic behaviour on CM-Sepadex gel, addition test, and change of electrophoretic mobility in human serum showed differences between human erythrocyte catalase and bovine liver catalase. These results suggest that human erythrocyte catalase and bovine liver catalase are two distinct catalase forms.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Human erytrocyte catalase purification molecular weight electrophoretic mobility isoelectric point absorption charateristics bovine liver catalase
Megjelenés:	Enzyme. - 41 : 4 (1989), p. 191-199. -
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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