Vigny M, Gisiger V, Massoulié J
Proc Natl Acad Sci U S A. 1978 Jun;75(6):2588-92. doi: 10.1073/pnas.75.6.2588.
"Nonspecific" cholinesterase (acylcholine acylhydrolase; EC 3.1.1.8) from various rat tissues has been found to exist in several stable molecular forms that appear as exact counterparts of molecular forms of acetylcholinesterase (acetylcholine hydrolase; EC 3.1.1.7). The sedimentation pattern of cholinesterase was similar to that of acetylcholinesterase with a small but significant shift between the sedimentation coefficients of the corresponding forms. Extraction yields in different media also demonstrated a close parallelism between the two enzyme systems. Other properties, such as thermal stability and catalytic characteristics, indicated both differences and similarities. In spite of the structural resemblance implied by their physicochemical properties, cholinesterase did not crossreact with antibodies against acetylcholinesterase. The nature of the relationships revealed by these studies and their bearing on the physiological significance of cholinesterases are discussed.
已发现来自各种大鼠组织的“非特异性”胆碱酯酶(酰基胆碱酰基水解酶;EC 3.1.1.8)以几种稳定的分子形式存在,这些形式似乎是乙酰胆碱酯酶(乙酰胆碱水解酶;EC 3.1.1.7)分子形式的精确对应物。胆碱酯酶的沉降模式与乙酰胆碱酯酶相似,相应形式的沉降系数之间存在微小但显著的差异。在不同介质中的提取产率也表明这两种酶系统之间存在密切的平行关系。其他特性,如热稳定性和催化特性,显示出差异和相似之处。尽管它们的物理化学性质暗示了结构上的相似性,但胆碱酯酶与抗乙酰胆碱酯酶抗体不发生交叉反应。讨论了这些研究所揭示的关系的性质及其对胆碱酯酶生理意义的影响。