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Structure Analysis of Streptococcal Protein G Fc Binding Domain
作者姓名:蔡仕英  王园园  姚志建
作者单位:Laboratory of Protein Chemistry,Institute of Basic Medical Sciences,P. O. Box 130(3),Beijing 100850,PRC,Laboratory of Protein Chemistry,Institute of Basic Medical Sciences,P. O. Box 130(3),Beijing 100850,PRC,Laboratory of Protein Chemistry,Institute of Basic Medical Sciences,P. O. Box 130(3),Beijing 100850,PRC
摘    要:The gene fragment (191 bp) encoding protein G IgG Fc binding domain was isolated by PCR from group G streptococcus (CMCC32138), and a clone containing this gene fragment was found to give fine reactivity to human IgG when expressed in Escherichia coli. The complete nucleotide sequence of the gene fragment was determined. One base pair differs from previously reported protein Gnucleotide sequences, and resultsin an amino acid change (Ala-Thr), but this variation makes no difference in binding to the IgG Fc part by ELISA.The secondary structure of the protein G IgG Fc binding domain has been estimated by circular dichroism and assigned by computer algorithm.It shows a typical α-helix region in this domain.By breaking this α-helix region with recombinant DNA techniques, a 44 peptide, which contained the N-terminal 27 amino acid residues of this domain, was expressed in E. coli and showed no reactivity to IgG.The hydropathicity of this domain was also analyzed and compared with that of protein A relevant


Structure Analysis of Streptococcal Protein G Fc Binding Domain
CAI Shi-Ying WANG Yuan-Yuan and YAO Zhi-Jian.Structure Analysis of Streptococcal Protein G Fc Binding Domain[J].Science in China(Chemistry),1993(1).
Authors:CAI Shi-Ying WANG Yuan-Yuan and YAO Zhi-Jian
Abstract:
Keywords:protein G Fc binding domain  DNA sequencing  eircular dichroism  structure predietion  binding mechanism  
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