教師資料查詢 | 類別: 期刊論文 | 教師: 陳銘凱 CHERN MING-KAI (瀏覽個人網頁)

標題:Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver - purification, characterization and comparison with human cytoplasmic E3 isozyme
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出版(發表)日期1999/06/01
作品名稱Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver - purification, characterization and comparison with human cytoplasmic E3 isozyme
作品名稱(其他語言)
著者Chern, Ming-kai; Pietruszko, Regina
單位淡江大學生命科學研究所
出版者Ottawa: NRC Research Press
著錄名稱、卷期、頁數Biochemistry and Cell Biology 77, pp.179-187
摘要Betaine aldehyde dehydrogenase has been purified to homogeneity from rat liver mitochondria. The properties of betaine aldehyde dehydrogenase were similar to those of human cytoplasmic E3 isozyme in substrate specificity and kinetic constants for substrates. The primary structure of four tryptic peptides was also similar; only two substitutions, at most, per peptide were observed. Thus, betaine aldehyde dehydrogenase is not a specific enzyme, as formerly believed; activity with betaine aldehyde is a property of aldehyde dehydrogenase (EC 1.2.1.3), which has broad substrate specificity. Up to the present time the enzyme was thought to be cytoplasmic in mammals. This report establishes, for the first time, mitochondrial subcellular localization for aldehyde dehydrogenase, which dehydrogenates betaine aldehyde, and its colocalization with choline dehydrogenase. Betaine aldehyde dehydrogenation is an important function in the metabolism of choline to betaine, a major osmolyte. Betaine is also important in mammalian organisms as a major methyl group donor and nitrogen source. This is the first purification and characterization of mitochondrial betaine aldehyde dehydrogenase from any mammalian species.
關鍵字Aldehyde;Betaine;Dehydrogenase;Mitochondria;Rat liver
語言英文
ISSN0829-8211
期刊性質國外
收錄於
產學合作
通訊作者Pietruszko, Regina
審稿制度
國別加拿大
公開徵稿
出版型式紙本
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