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Shigenori Yaguchi, Tetsuya Nakajima, Toshihisa Sumi, Naoki Yamauchi, and Masayoshi Shigyo

of the second PCR products was incubated for 2 h at 37 °C in a volume of 15 μL using 2 U of a restriction enzyme and subsequently resolved by 5% denaturing polyacrylamide gel electrophoresis (PAGE) with silver staining according to the procedure of

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Xiu Cai Fan, Hai Sheng Sun, Ying Zhang, Jian Fu Jiang, Min Li, and Chong Huai Liu

annealing temperature because of the different primers used. The amplification products were separated using 8% polyacrylamide gel electrophoresis at 75 W (Bio-Rad Electrophoresis system, Hercules, CA) for 2 h and then visualized using a simplified silver

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Ying Li, Liyi Zhang, Zhen Zhang, Peihua Cong, and Zong-Ming Cheng

extension at 72 °C for 1 min followed by a final extension at 72 °C for 10 min. The PCR products were resolved by 6% polyacrylamide gel electrophoresis. Before loading, the samples were denatured at 94 °C for 5 min. The gel was stained with silver nitrate

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Aoxue Wang, Fanjuan Meng, Xiangyang Xu, Yong Wang, and Jingfu Li

/volume) agarose gel containing ethidium bromide 1.0 μg·mL –1 in 1 × TAE (40 m m Tris-acetate, 1 m m EDTA) buffer, observed under ultraviolet light and photographed. SSR PCR products were separated by polyacrylamide gel electrophoresis (6% gel) and silver

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Alexis K. Nagel, Guido Schnabel, Cesar Petri, and Ralph Scorza

gel electrophoresis was performed on total cellular protein using a Mini-Protean ® 3 with 18% Tris-HCl Ready Gels (Bio-Rad Laboratories, Hercules, CA). Proteins were transferred to an immunoblot polyvinyl difluoride membrane using a Mini

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Mark K. Ehlenfeldt and James J. Polashock

) . Polymerase chain reactions, polyacrylamide gel electrophoresis, and silver staining were as described ( Novy et al., 1994 ). Reliable polymorphic bands were scored as 1 (present) or 0 (absent). Cluster analysis and tree generation using NTSYS-pc (Exeter

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Hetal M. Kalariya, Guido Schnabel, Cesar Petri, and Ralph Scorza

μg) was used to perform sodium dodecyl sulfate–polyacrylamide gel electrophoresis using 15% Tris-HCl ready Gels (Bio-Rad Laboratories, Hercules, CA). Protein was transferred to an immunoblot polyvinylidene fluoride membrane (Bio-Rad Laboratories), and

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Yanbin Su, Yumei Liu, Huolin Shen, Xingguo Xiao, Zhansheng Li, Zhiyuan Fang, Limei Yang, Mu Zhuang, and Yangyong Zhang

45 s at 72 °C, and a final extension for 7 min at 72 °C. PCR amplifications were carried out in a GeneAmp PCR system 9700 (Applied Biosystems, Foster City, CA). The resulting products were subjected to 8% polyacrylamide gel electrophoresis at 160 V

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Olfa Zarrouk, Pilar S. Testillano, María Carmen Risueño, María Ángeles Moreno, and Yolanda Gogorcena

volume of 1 mL, as described by Fernández-García et al. (2004) . The mean value of at least three replications was taken as indicator of peroxidase activity. Determination of isoperoxidase profile by native polyacrylamide gel electrophoresis (PAGE

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Huiling Wang, Wei Wang, Weidong Huang, and Haiying Xu

/v) polyvinylpyrrolidone. Protein concentration was determined as described in Bardford (1976) using bovine serum albumin as the standard. The separation of total proteins was performed using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) in 12