Oka K, Kojima K, Nagatsu T
Biochem Int. 1983 Sep;7(3):387-93.
Tyrosine hydroxylase purified to apparent homogeneity from the soluble fraction of bovine adrenal medulla had an apparent Mr of about 280,000 by Bio-Gel A-1.5m chromatography, and gave a single band with a Mr of 60,000 by sodium dodesyl sulfate polyacrylamide gel electrophoresis. The enzyme is considered to be composed of four identical subunits. Isoelectric point of purified enzyme was pH 6.0. The amino acid composition of the enzyme was characterized by fairly high contents of glutamic acid and alanine residues. The N-terminal amino acid was determined to be glutamic acid.
从牛肾上腺髓质可溶性部分纯化至表观均一的酪氨酸羟化酶,通过Bio-Gel A-1.5m色谱法测得其表观分子量约为280,000,而通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳显示为一条单一的条带,分子量为60,000。该酶被认为由四个相同的亚基组成。纯化酶的等电点为pH 6.0。该酶的氨基酸组成特点是谷氨酸和丙氨酸残基含量相当高。测定其N端氨基酸为谷氨酸。