Anderson W M, Fisher R R
Biochim Biophys Acta. 1981 Mar 12;635(1):194-9. doi: 10.1016/0005-2728(81)90018-9.
Reaction of purified bovine heart transhydrogenase with bifunctional cross-linking reagents dimethyl adipimidate, dimethyl pimelimidate, dimethyl suberimidate, and dithiobis(succinimidyl propionate) results in the appearance of a dimer band on sodium dodecyl sulfate polyacrylamide gels with no higher oligomers formed. Treatment of the enzyme with 6 M urea led to inactivation and prevented cross-linking by dimethyl suberimidate. Transhydrogenase reconstituted into phosphatidylcholine proteoliposomes also yielded a dimer band on cross-linking. These data indicate that soluble and functionally reconstituted transhydrogenase possesses a dimeric structure.
纯化的牛心转氢酶与双功能交联剂己二酸二甲酯、庚二酸二甲酯、辛二酸二甲酯和二硫代双（琥珀酰亚胺丙酸酯）反应，导致在十二烷基硫酸钠聚丙烯酰胺凝胶上出现二聚体条带，且未形成更高的寡聚体。用6 M尿素处理该酶会导致其失活，并阻止辛二酸二甲酯的交联作用。重构到磷脂酰胆碱蛋白脂质体中的转氢酶在交联时也产生了一条二聚体条带。这些数据表明，可溶性且功能重构的转氢酶具有二聚体结构。
