Gasparis M S, Yang W H, Klein R L
Neurochem Res. 1983 Nov;8(11):1417-39. doi: 10.1007/BF00964998.
Bovine splenic nerve and adrenal medulla were used as homologous sources of dopamine beta-hydroxylase permitting the isolation of enzyme specific to a purified fraction of large dense cored noradrenergic vesicles and chromaffin granules, respectively. The hydrophilic (water soluble) form of the enzyme was purified to homogeneity on the bases of gel electrophoresis, isoelectric focusing, and double immunodiffusion tests from the physical lysates of the vesicles and granules. Amino acid analyses suggest that the hydrophilic dopamine beta-hydroxylase is the predominant form in the nerve vesicles. It has higher neutral and lower hydrophobic amino acid group residues when compared to the adrenomedullary enzyme prepared in this and most other laboratories. Among the neutral amino acids, this difference appears to reflect approximately 40% higher serine and glycine contents, and among the hydrophobic amino acids it may reflect in part approximately 25% lower leucine content. Although the terms hydrophilic and amphiphilic can be properly applied to certain chemical properties of the D beta H forms, it is not at all certain that these terms can be used quantitatively to describe the matrix and membrane associated forms of the enzyme, respectively.
牛脾神经和肾上腺髓质被用作多巴胺β-羟化酶的同源来源，从而分别允许分离出对大致密核心去甲肾上腺素能囊泡和嗜铬颗粒的纯化部分具有特异性的酶。该酶的亲水性（水溶性）形式通过凝胶电泳、等电聚焦以及来自囊泡和颗粒物理裂解物的双向免疫扩散试验纯化至同质。氨基酸分析表明，亲水性多巴胺β-羟化酶是神经囊泡中的主要形式。与在本实验室和大多数其他实验室制备的肾上腺髓质酶相比，它具有更高的中性氨基酸和更低的疏水氨基酸基团残基。在中性氨基酸中，这种差异似乎反映丝氨酸和甘氨酸含量大约高40%，而在疏水氨基酸中，它可能部分反映亮氨酸含量大约低25%。尽管亲水性和两亲性这两个术语可以恰当地应用于多巴胺β-羟化酶形式的某些化学性质，但完全不确定这些术语是否可以分别用于定量描述该酶与基质和膜相关的形式。
