Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver - purification, characterization and comparison with human cytoplasmic E3 isozyme
學年 87
學期 2
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 en
ISSN 0829-8211
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 CAN
公開徵稿
出版型式 紙本
相關連結

機構典藏連結 ( http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/61852 )

機構典藏連結