粉状孢霉白腐真菌中纤维二糖醌脱氢酶多种形式的分离、纯化及某些性质
Resolution, purification and some properties of the multiple forms of cellobiose quinone dehydrogenase from the white-rot fungus Sporotrichum pulverulentum.
作者信息
Morpeth F F, Jones G D
出版信息
Biochem J. 1986 May 15;236(1):221-6. doi: 10.1042/bj2360221.
Abstract
Four forms of cellobiose quinone dehydrogenase have been purified from the white-rot fungus Sporotrichum pulverulentum. The Mr of the enzyme has been estimated by sedimentation equilibrium to be 57,800 and by SDS/polyacrylamide-gel to be 60,000. These enzymes are clearly monomers. Cellobiose quinone dehydrogenases contain FAD and variable amounts of a green chromophore which we suggest is 6-hydroxy-FAD. The superoxide anion and H2O2 are the products of its reaction with oxygen. All of the isoenzymes from any one preparation display similar kinetic parameters. However, these vary between preparations. The only apparent difference between the four separable isoenzymes is their neutral-sugar content.
摘要
已从白腐真菌粉状孢霉中纯化出四种纤维二糖醌脱氢酶。通过沉降平衡法估算该酶的相对分子质量为57,800，通过SDS/聚丙烯酰胺凝胶法估算为60,000。这些酶显然是单体。纤维二糖醌脱氢酶含有黄素腺嘌呤二核苷酸（FAD）和数量不等的绿色发色团，我们认为其为6-羟基-FAD。超氧阴离子和过氧化氢是其与氧气反应的产物。任一制剂中的所有同工酶都表现出相似的动力学参数。然而，不同制剂之间这些参数有所不同。四种可分离的同工酶之间唯一明显的差异是它们的中性糖含量。
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