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Purificatin and characterization of unidentified biotin-containing enzymes in rice

등록일
2006년 9월 11일 10시 51분 21초
접수번호
1293
발표코드
28P279포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
반상오, 최원기, 정제훈
전남대학교 화학과,
The biotin-containing enzymes have been known from diverse plants. Biotin is a water-soluble vitamin that serves as cofactor for biotin-dependent enzymes which catalyze carboxylation. The biotin is covalently bound to a lysine residue of these enzymes. The biotin-containing proteins from rice leaves were partly purified by affinity chromatography and ion-exchange chromatography using Cibacron Blue F3GA-sepharose and monoQ, respectively. The fractions containing biotin proteins were detected by Western Blotting. Subsequently, the biotin fractions were analyzed by 2D SDS-PAGE. The amino acid sequences of protein bands expected to contain biotin through Western Blotting were determined by de novo sequencing of tryptic peptides using a tandem mass spectrometry. A variety of previously unidentified proteins were shown to contain biotin. The method described in this communication is very prospective for screening new bicarbonate-metabolizing enzymes.

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