title: Shotgun analysis on the peritrophic membrane of the silkworm Bombyx mori.
abstract: The insect midgut epithelium is generally lined with a unique chitin and protein structure, the peritrophic membrane (PM), which facilitates food digestion and protects the gut epithelium. We used gel electrophoresis and mass spectrometry to identify the extracted proteins from the silkworm PM to obtain an in-depth understanding of the biological function of the silkworm PM components. A total of 305 proteins, with molecular weights ranging from 8.02 kDa to 788.52 kDa and the isoelectric points ranging from 3.39 to 12.91, were successfully identified. We also found several major classes of PM proteins, i.e. PM chitin-binding protein, invertebrate intestinal mucin, and chitin deacetylase. The protein profile provides a basis for further study of the physiological events in the PM of Bombyx mori.
authors.affiliation: State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China.
authors.forename: Xiaowu
authors.initials: X
authors.lastname: Zhong
authors.forename: Liping
authors.initials: L
authors.lastname: Zhang
authors.forename: Yong
authors.initials: Y
authors.lastname: Zou
authors.forename: Qiying
authors.initials: Q
authors.lastname: Yi
authors.forename: Ping
authors.initials: P
authors.lastname: Zhao
authors.forename: Qingyou
authors.initials: Q
authors.lastname: Xia
authors.forename: Zhonghuai
authors.initials: Z
authors.lastname: Xiang
mesh_terms: D000818:Animals; D012831:Bombyx / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D019295:Computational Biology; D004064:Digestive System / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D019476:Insect Proteins / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D040901:Proteomics; D053719:Tandem Mass Spectrometry
chemical_list: D019476:Insect Proteins; D008565:Membrane Proteins