Cleeter M W, Banister S H, Ragan C I
Biochem J. 1985 Apr 15;227(2):467-74. doi: 10.1042/bj2270467.
The structure of bovine heart mitochondrial NADH dehydrogenase was investigated by using two cleavable cross-linking agents, disuccinimidyl tartrate and (ethylene glycol)yl bis-(succinimidyl succinate). Cross-linking was analysed primarily by immunoblotting to detect products containing subunits of the iron-protein fraction from chaotropic resolution of the enzyme, namely those of 75, 49, 30 and 13 kDa. By using both the isolated iron-protein fraction and the intact dehydrogenase, cross-links were identified between these four subunits, from these subunits to the largest subunit of the flavoprotein fraction, which contains the active site for NADH, and from these subunits to polypeptides in the hydrophobic shell, which surrounds the hydrophilic iron-protein and flavoprotein fractions.
通过使用两种可裂解的交联剂酒石酸二琥珀酰亚胺酯和双（琥珀酰亚胺基琥珀酸酯）（乙二醇）酯，对牛心线粒体NADH脱氢酶的结构进行了研究。交联主要通过免疫印迹进行分析，以检测在该酶的离液分辨率下含有铁蛋白部分亚基的产物，即75、49、30和13 kDa的亚基。通过使用分离的铁蛋白部分和完整的脱氢酶，确定了这四个亚基之间、这些亚基与黄素蛋白部分的最大亚基（其含有NADH的活性位点）之间以及这些亚基与围绕亲水性铁蛋白和黄素蛋白部分的疏水壳中的多肽之间的交联。
