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Identification and characterization of two chitin‐binding proteins from the peritrophic membrane of the silkworm, Bombyx mori L.
Author(s) -
Yang HuaJun,
Zhou Fang,
Malik Firdose Ahmad,
Bhaskar Roy,
Li XingHua,
Hu JiaBiao,
Sun ChunGuang,
Miao YunGen
Publication year - 2010
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20389
Subject(s) - bombyx mori , chitin , biology , biochemistry , western blot , midgut , amino acid , cysteine , peptide sequence , bombyx , molecular mass , recombinant dna , microbiology and biotechnology , gene , botany , larva , enzyme , chitosan
The peritrophic membrane (PM) is a semi‐permeable lining of the insect midgut, broadly analogous to the mucous lining of vertebrate gut. The PM proteins are important achievements for the function of the PM. In this study, two chitin‐binding proteins ( Bm PM‐P43 and Bm PM‐P41) from the PM of the silkworm, Bombyx mori, were identified and cloned. These proteins showed the molecular mass of 43 and 41 kDa, respectively. The deduced amino acid sequences codes for a protein of 381 amino acid residues and 364 amino acid residues, containing 12 and 14 cysteine residues followed by similar domain, both of them have 5 cysteine residues in similar position in the C‐terminal. The confirmation of these proteins was performed by western blot analysis of recombinant Bm PM‐P43 and Bm PM‐P41. The chitin‐binding activity analysis showed that the Bm PM‐P43 and Bm PM‐P41 could bind to chitin strongly. It is concluded that Bm PM‐P43 and Bm PM‐P41 contains a polysaccharide deacetylase domain instead of peritrophin domain, indicated that these two proteins may belong to a new chitin‐binding protein family. © 2010 Wiley Periodicals, Inc.