Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules: Relation to soluble dopamine β-monooxygenase☆
Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules: Relation to soluble dopamine β-monooxygenase☆
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从嗜铬颗粒中纯化膜结合多巴胺β-单加氧酶：与可溶性多巴胺β-单加氧酶的关系☆
DOI：
10.1016/0003-9861(81)90456-2
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发表时间：
1981
影响因子：
3.9
通讯作者：
R. Hogue
中科院分区：
文献类型：
--
作者：
E. Slater;S. Zaremba;R. Hogue
膜结合多巴胺β-单加氧酶（MDBH）用乳化剂（一种非离子去污剂）增溶，并通过一步阴离子交换层析在DEAE-纤维素上纯化。还原和变性MDBH的分子量约为75，000。未还原的MDBH的分子量是其两倍。MDBH和SDBH（可溶性多巴胺β-单加氧酶）具有许多相似的特征。使用SDBH的抗血清，这两种蛋白质在免疫扩散测定中显示出同一性反应。它们的色谱、电泳和分子量特征也非常相似。虽然MDBH和SDBH的氨基酸组成没有不同，但MDBH组成中某些氨基酸的含量较高，特别是疏水性氨基酸。尽管MDBH和SDBH的显著相似性在上文和通过分析肽图谱证明，但可在MDBH中检测到在SDBH中未发现的肽。
Membrane-bound dopamine β-monooxygenase (MDBH) has been solubilized using emulphogen, a nonionic detergent, and purified by a single-step anion-exchange chromatography on DEAE-cellulose. Reduced and denatured MDBH has a molecular weight of approximately 75,000. The unreduced MDBH has a molecular weight twice that size. MDBH and SDBH (soluble dopamine β-monooxygenase) possess many similar features. Using antiserum to SDBH, the two proteins show a reaction of identity in immunodiffusion assays. Their chromatographic, electrophoretic, and molecular weight characteristics are also very similar. Although the amino acid compositions of MDBH and SDBH were not dissimilar, the MDBH composition had a higher content of certain amino acids, particularly hydrophobic ones. Despite the remarkable likeness of MDBH and SDBH demonstrated above and by analytical peptide maps, peptides can be detected in MDBH which are not found in SDBH.