title: [Expression, Purification and Bioinformatics Analysis of β-hexosaminidase of Dermatophagoides farinae].
abstract: The DNA fragment encoding β-hexosaminidase was synthesized, and cloned into pET-28a vector. The constructed plasmid pMD18-T-β-hexosaminidase was transformed into E. coli Top 10 and followed by expression of the protein induced by IPTG. SDS-PAGE result showed that the relative molecular mass of the recombinant protein was about M, 55 000. The full length of β-hexosaminidase gene was 1 410 bp. Bioinformatics analysis revealed that β-hexosaminidase was composed with 469 amino acid residues with a calculated molecular weight of Mr 55,000, and its secondary structure was composed of strand (14.71%), helix (30.70%), and loop (54.58%). β-hexosaminidase was a hydrophilic protein without signal peptide, and located in the extracellular space.
authors.forename: Li-hua
authors.initials: LH
authors.lastname: Mo
authors.forename: Yu-lin
authors.initials: YL
authors.lastname: Liu
authors.forename: Li-tao
authors.initials: LT
authors.lastname: Yang
authors.forename: Xiao-qin
authors.initials: XQ
authors.lastname: Fan
authors.forename: Zhi-gang
authors.initials: ZG
authors.lastname: Liu
authors.forename: Ping-chang
authors.initials: PC
authors.lastname: Yang
mesh_terms: D000818:Animals; D019295:Computational Biology; D040001:Dermatophagoides farinae; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D005822:Genetic Vectors; D010957:Plasmids; D011994:Recombinant Proteins; D001619:beta-N-Acetylhexosaminidases
chemical_list: D011994:Recombinant Proteins; D001619:beta-N-Acetylhexosaminidases