作者: B.N. La Du , B. Dewald
DOI: 10.1016/S0065-2571(71)80052-3
关键词: Biology 、 Active center 、 Molecular mass 、 Enzyme 、 Cholinesterase 、 Esterase 、 Dibucaine 、 Biochemistry 、 Protein primary structure 、 Choline 、 Molecular medicine 、 Genetics 、 Cancer research 、 Molecular biology
摘要: Summary Individual variation in response to succinylcholine has stimulated investigations on the variations and genetic control of serum cholinesterase man. It been found that level varies from essentially no detectable activity exceedingly high levels due a number different mutations. Qualitative esterase are also inherited. The most common variant latter type is atypical (dibucaine resistant) which differs normal its lower apparent affinity for choline ester substrates inhibitors. On basis evidence derived kinetic experiments, both anionic site esteratic modified. These changes may be difference primary structure enzyme at one position affects sites active center enzyme. modified properties expressed major component (C4) minor components (C1, C2 C3) present multiple molecular forms. Component C4 (molecular weight about 300,000) can converted C3 by treatment with urea, transformed C1-like sulfhydryl reagents. Both C1 (native derived) have weights 80,000 approximately one-fourth as large C4. This information should useful further studies forms how structural alterations account altered cholinesterases.