作者: R Hoeldtke , S Kaufman
DOI: 10.1016/S0021-9258(17)40366-8
关键词: Biochemistry 、 Differential centrifugation 、 Phospholipid 、 Molecular biology 、 Cofactor 、 Chymotrypsin 、 Enzyme 、 Chemistry 、 Tyrosine hydroxylase 、 Sodium 、 Phosphorylation 、 Cell biology
摘要: Bovine adrenal tyrosine hydroxylase has been obtained in a form that is 85 to 90% pure. Sodium dodecyl sulfate-gel electrophoresis and density gradient centrifugation studies have established the subunit molecular weight of chymotrypsin-solubilized enzyme 34,000. The presence iron purified (0.50 0.75 mol iron/mol enzyme) established. Crude particulate can be activated by phospholipid, phosphatidyl-L-serine, or exposure enzymatic phosphorylating conditions. Both forms activation lower Km for its 2-amino-4-hydroxypteridine cofactor. By contrast, solubilized chymotrypsin cannot either these methods.