Korean Journal of Microbiology (미생물학회지)
- Volume 31 Issue 3
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- Pages.237-244
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- 1993
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- 0440-2413(pISSN)
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- 2383-9902(eISSN)
Characterization of Aspartate Aminotransferase Purified from Streptomyces fradiae
Streptomyces fradiae에서 분리된 Aspartate Aminotransferase의 특성
- Lee, Sang-Hee (Department of Microbiology, College of Natural Sciences, Seoul National University) ;
- Lee, Kye-Joon (Department of Microbiology, College of Natural Sciences, Seoul National University)
- Published : 1993.06.01
Abstract
Aspartate aminotransferase (ASAT) (L-aspartate : 2-oxyoglutarate, EC 2.6. 1. 1.) from Streptomyces fradiae NRRL 2702 has been purified by acetone precipitation, DEAE-cellulose, hydroxyapatite, and preparative electrophoresis (Prep cell), of which the last was the most effective step in the purification of ASAT. The molecular mass was estimated to be 54,000 dalton by SDS-PAGE and 120,000 dalton by gel filtration chromatography. Preparative isoelectric focusing of purified ASAT resulted in one polypeptide band with a pI of 4.2, showing homogeneity and indicating that the enzyme is composed of two identical subunits. The enzyme was specific for L-aspartate as an amino donor ; the