Armesilla A L, Thurston C F, Yagüe E
Division of Life Sciences, King's College London, London, UK.
FEMS Microbiol Lett. 1994 Mar 1;116(3):293-9. doi: 10.1111/j.1574-6968.1994.tb06718.x.
The cel1 gene of Agaricus bisporus encodes a protein (CEL1) that has an architecture resembling the multi-domain fungal cellulases, although the sequence of its putative catalytic core is not matched by any other in the protein and nucleic acid data bases. The N-terminal half of the putative catalytic domain of CEL1 was expressed in Escherichia coli as a fusion protein with glutathione-S-transferase. The fusion protein was used to raise a CEL1-specific antibody. CEL1 was detected as an extracellular 49.8 kDa protein in A. bisporus cellulose-grown cultures, where it bound strongly to cellulose. CEL1 was neither an endoglucanase, a cellobiohydrolase able to hydrolyze fluorogenic cellobiosides, a beta-glucosidase, a xylanase, nor a cellobiose: quinone oxidoreductase. CEL1 was present in some fractions of culture fluid separated by electrophoresis which released soluble sugars from crystalline cellulose.
双孢蘑菇的cel1基因编码一种蛋白质（CEL1），其结构类似于多结构域真菌纤维素酶，尽管其假定催化核心的序列在蛋白质和核酸数据库中与其他序列均不匹配。CEL1假定催化结构域的N端一半在大肠杆菌中作为与谷胱甘肽-S-转移酶的融合蛋白表达。该融合蛋白用于制备CEL1特异性抗体。在双孢蘑菇纤维素培养物中，CEL1被检测为一种细胞外49.8 kDa的蛋白质，它与纤维素紧密结合。CEL1既不是内切葡聚糖酶、能够水解荧光纤维二糖苷的纤维二糖水解酶、β-葡萄糖苷酶、木聚糖酶，也不是纤维二糖：醌氧化还原酶。CEL1存在于通过电泳分离的部分培养液中，这些部分能从结晶纤维素中释放出可溶性糖。
