Purification and Amino Acid Sequence of the Linoleate Isomerase Produced from Butyrivibrio fibrisolvens A-38

  • Park, Sook-Jahr (Dept. of Agricultural Chemistry and Gyeongsang Institute of Cancer Research, Gyeongsang National University Chinju 660-701) ;
  • Park, Kyung-Ah (Dept. of Agricultural Chemistry and Gyeongsang Institute of Cancer Research, Gyeongsang National University Chinju 660-701) ;
  • Park, Cjerl-Woo (Dept. of Agricultural Chemistry and Gyeongsang Institute of Cancer Research, Gyeongsang National University Chinju 660-701) ;
  • Park, Won-Seck (Dept. of Agricultural Chemistry and Gyeongsang Institute of Cancer Research, Gyeongsang National University Chinju 660-701) ;
  • Kim, Jeong-Ok (H&K Laboratiories, Chinju 660-250) ;
  • Ha, Yeong-Lae (Dept. of Agricultural Chemistry and Gyeongsang Institute of Cancer Research, Gyeongsang National University Chinju 660-70)
  • 발행 : 1996.10.01

초록

Molecular weight and partial amino acid sequence of the cis, 9-cis, 12-octadecadienoate isomerase(linoleate isomerase) of Butyrivibrio fibrisovens A-38 were determined. Linoleate isomerase was isolated from the bac-teria cultured anaerobically and purified by ultracentrifugation in conjunction with Sepharose 6B column chro-matography, Phenyl sepharose 4B column chromatography and fast performance liquid chromatography (EPLC). The isomerase was single polypeptide with 19KD of molecular weight, when determined by SDS-PAGE. Fourteen amino acids sequence of N-terminal of the linoleate isomerase was N-GEIDKYPRIIKQQ determined by Edman method.

키워드

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