Kohlmiller N A, Howard J B
J Biol Chem. 1979 Aug 10;254(15):7309-15.
The complete primary structure of the alpha subunit of protocatechuate 3,4-dioxygenase has been determined by automated Edman degradation and carboxypeptidase digestionof the intact alpha chain and of peptides derived from trypsin (N.A. Kohlmiller and J.B. Howard (1979) J. Biol. Chem. 254, 7302-7308) and Staphylococcus aureus protease digestion, and from hydroxylamine and dilute acid cleavage. The alpha chain was found to consist of 200 residues in the following sequence from the NH2-terminal end: (formula: see text).
通过对完整的α链以及源自胰蛋白酶（N.A.科尔米勒和J.B.霍华德（1979年）《生物化学杂志》254卷，7302 - 7308页）和金黄色葡萄球菌蛋白酶消化产物、羟胺和稀酸裂解产物的肽段进行自动Edman降解和羧肽酶消化，已确定原儿茶酸3,4 - 双加氧酶α亚基的完整一级结构。发现α链由200个残基组成，从NH2末端起的序列如下：（分子式：见正文）
