Brophy P M, Ben-Smith A, Behnke J M, Brown A, Pritchard D I
Pharmacy Department, School of Applied Sciences, De Montfort University, Leicester, United Kingdom.
J Parasitol. 1995 Apr;81(2):302-3.
A glutathione-affinity matrix was used to identify glutathione-dependent protein(s) in somatic extracts of the nematode Heligmosomoides polygyrus. Polypeptides of 70-80 kDa were retained by the affinity matrix following the elution of H. polygyrus glutathione S-transferases by 5 mM glutathione. The 70-80-kDa polypeptides were subsequently eluted from the matrix by the addition of 20 mM glutathione and these polypeptides did not show glutathione S-transferase activity. The high-affinity H. polygyrus glutathione-binding proteins may be related to the uncharacterized purification hindering factors previously demonstrated during the isolation of glutathione S-transferases in several other helminths.
使用谷胱甘肽亲和基质来鉴定多枝细颈线虫体细胞提取物中的谷胱甘肽依赖性蛋白。在用5 mM谷胱甘肽洗脱多枝细颈线虫谷胱甘肽S-转移酶后，70-80 kDa的多肽被亲和基质保留。随后通过添加20 mM谷胱甘肽从基质中洗脱70-80 kDa的多肽，并且这些多肽未显示出谷胱甘肽S-转移酶活性。多枝细颈线虫高亲和力的谷胱甘肽结合蛋白可能与先前在其他几种蠕虫中分离谷胱甘肽S-转移酶时所证明的未表征的纯化阻碍因子有关。
