Basu Arghya, Chaudhuri Paramita, Malakar Dipankar, Ghosh Anil K
Biotechnology Division, Indian Institute of Chemical Biology, Kolkata 700 032, India.
Biotechnol Lett. 2008 Feb;30(2):299-304. doi: 10.1007/s10529-007-9535-y. Epub 2007 Sep 26.
An electrophoretically homogenous aggregate of acid trehalase, invertase and an unidentified 37-41 kDa protein was purified from Saccharomyces cerevisiae. N-terminal analysis of the protein revealed an amino acid sequence identical to that of Bgl2p (endo-beta-l,3-glucanase) of S. cerevisiae. Acid trehalase activity with co-eluted glucanase activity was observed from late growth phase through early stationary phase. Pools with high percentage of Bgl2p corresponded with high acid trehalase activity. A BGL2 deletion strain had lower acid trehalase activity. The 37-41 kDa protein represents Bgl2p which, besides imparting glucanase activity, could also be acting as a regulator for the acid trehalase activity by association in the enzyme aggregate.
从酿酒酵母中纯化出了一种由酸性海藻糖酶、转化酶和一种未鉴定的37 - 41 kDa蛋白质组成的电泳均一聚集体。对该蛋白质的N端分析显示其氨基酸序列与酿酒酵母的Bgl2p（内切β-1,3-葡聚糖酶）相同。从生长后期到稳定期早期均观察到与共洗脱的葡聚糖酶活性相关的酸性海藻糖酶活性。Bgl2p比例高的组分对应着高酸性海藻糖酶活性。BGL2缺失菌株的酸性海藻糖酶活性较低。这种37 - 41 kDa的蛋白质代表Bgl2p，它除了具有葡聚糖酶活性外，还可能通过在酶聚集体中的结合作用作为酸性海藻糖酶活性的调节剂。
