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使用特异性多克隆抗体研究来自酒类酒球菌及其他乳酸菌的苹果酸乳酸酶。

Using specific polyclonal antibodies to study the malolactic enzyme from Leuconostoc oenos and other lactic acid bacteria.

作者信息

Labarre C, Cavin J F, Diviès C, Guzzo J

机构信息

Laboratory of Microbiology, ENSBANA, Dijon, France.

出版信息

Lett Appl Microbiol. 1998 Apr;26(4):293-6. doi: 10.1046/j.1472-765x.1998.00331.x.

Abstract

Specific polyclonal antibodies directed against the malolactic enzyme of Leuconostoc oenos were obtained. Despite the homologies between the malolactic enzymes from Leuc. oenos and Lactococcus lactis, no immunological relationship was detected with the L. lactis malolactic enzyme, suggesting differences in their structural organization. The use of the antiserum also demonstrated that the problem of heterologous expression occurring in the recombinant Escherichia coli strain (Labarre et al. 1996a) resulted in a low synthesis of the malolactic enzyme from Leuc. oenos. Moreover, a small amount of the protein was found to be peripherally associated to the membrane of Leuc. oenos.

摘要

获得了针对酒酒球菌苹果酸-乳酸酶的特异性多克隆抗体。尽管酒酒球菌和乳酸乳球菌的苹果酸-乳酸酶之间存在同源性,但未检测到与乳酸乳球菌苹果酸-乳酸酶的免疫关系,这表明它们的结构组织存在差异。抗血清的使用还表明,重组大肠杆菌菌株(拉巴尔等人,1996a)中出现的异源表达问题导致酒酒球菌苹果酸-乳酸酶的合成量较低。此外,还发现少量该蛋白质与酒酒球菌的细胞膜外周相关。

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