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- Title
桦褐孔菌酸性蛋白酶的基因克隆及其在菌核中的表达.
- Authors
李健; 王鑫; 胡志强; 亢学平; 杜忠伟; 王旭; 陈艳秋
- Abstract
The acid protease gene fromInonotus obliquus(IO-AP)was codon optimized, assembled into the expression vector pGEX-4T1-IO-AP and then expressed in Escherichia coli BL21(DE3)as inclusion body with a relative molecular weight of 60 kDa. This recombinant acid protease rIO-AP was then used as a high purity antigen to produce polyclonal antibodies of rIO-AP by the traditional 3-2-2-2 immunization method. Four Balb/c mice were immunized and antiserum titers were determined by the indirect ELISA method. After four times of immunization, all four mice contained antiserum titers greater than 121500, suggesting successful production of the rIO-AP polyclonal antibody. The resultant rIO-AP polyclonal antibodies were then used to analyze the expression profile of acid protease in Inonotus obliquus sclerotium by Western blot. The results showed that the expression of IO-AP in sclerotium reached a peak when sclerotia grew to 1.33 g.
- Publication
Acta Edulis Fungi, 2018, Vol 25, Issue 2, p42
- ISSN
1005-9873
- Publication type
Article
- DOI
10.16488/j.cnki.1005-9873.2018.02.005