摘要
对链霉亲和素进行纯化、鉴定，采用冷钝化的方法去除培养液中大部分杂蛋白，用亲和层析法从链霉菌L-183的培养液中纯化链霉亲和素（SA），经试验，SA回收率为75％～85％。鉴定表明，自制SA的分子量为74．5kD，每分子SA可结合3．2个生物素分子，活性为11．2U／mg，pI为7．4。自制SA各项生物学性质与文献报道相符。
The aim of this research is to refine the protocol of purification of SA and identify the character of SA. By utilizing the cold-denaturing method, most of other kinds of protein were screened out and SA was purified from the fermentation broth of L-183 by Using the refined affinity chromatography method. The rate of recollection was checked to be 75% - 85%. By identification, it is indicated that the molecular weight of self-mode SA was 74. 5 kD, the biotin-combining number 3.2, the activity 11.2u/mg, the pI around 7.4. So, the essential characters of SA are same as described by documents.
出处
《微生物学通报》
CAS
CSCD
北大核心
2006年第5期112-116,共5页
Microbiology China
基金
河北省科技厅专项基金资助项目
关键词
链霉亲和素
纯化鉴定
亲和层析
Streptavidin, Purification and identification, Affinity chromatography
