Wallace E F, Lovenberg W
Proc Natl Acad Sci U S A. 1974 Aug;71(8):3217-20. doi: 10.1073/pnas.71.8.3217.
Dopamine beta-hydroxylase [EC 1.14.17.1; 3,4-dihydroxyphenylethylamine, ascorbate:oxygen oxidoreductase (beta-hydroxylating)], a glycoprotein, was found to interact strongly with the plant lectin, concanavalin A. This interaction did not appear to alter the catalytic properties of the enzyme and did not prevent interaction of the protein with specific antibodies. Dopamine-beta-hydroxylase is adsorbed to concanavalin A covalently bound to Sepharose and can be eluted with alpha-methylmannoside. The enzyme is catalytically active when it is immobilized on a concanavalin A-Sepharose column. Enzymic removal of four of seven mannose residues present in the monomer does not result in the loss of any catalytic activity. It is concluded that the active site is not near the point of carbohydrate attachment on the molecule and that this may be of significance in orienting the enzyme on the vesicular membrane.
多巴胺β-羟化酶[EC 1.14.17.1；3,4-二羟基苯乙胺，抗坏血酸：氧氧化还原酶（β-羟化）]，一种糖蛋白，被发现与植物凝集素伴刀豆球蛋白A强烈相互作用。这种相互作用似乎并未改变该酶的催化特性，也未阻止该蛋白与特异性抗体的相互作用。多巴胺-β-羟化酶可被吸附到与琼脂糖共价结合的伴刀豆球蛋白A上，并可用α-甲基甘露糖苷洗脱。当该酶固定在伴刀豆球蛋白A-琼脂糖柱上时具有催化活性。酶促去除单体中七个甘露糖残基中的四个不会导致任何催化活性的丧失。得出的结论是，活性位点不在分子上碳水化合物附着点附近，这可能对该酶在囊泡膜上的定向具有重要意义。
