title: Analysis of the cuticular collagens of Ascaris suum.
abstract: The nematode cuticle is an extracellular structure composed mainly of collagens, with an insoluble epicuticle on the surface. The extracted collagens from adult Ascaris suum can be separated by SDS-PAGE into three major groups of polypeptides with apparent molecular masses of 34, 60-70 and 120-140 kDa. Densitometric evaluation of the polypeptide bands indicated that the three groups are present in the ratio of 1:2:6. Rotary shadowing of reduced, extracted molecules showed fibers 45 nm in length. This length is in excellent agreement with the calculated total length of amino acids in (Gly-X-Y) regions deduced from the collagen gene sequence of Caenorhabditis elegans and A. suum. It is proposed that the three groups of collagen polypeptides found in SDS-PAGE correspond to collagen monomers, dimers and trimers, and that the molecules in the dimeric and trimeric forms are cross-linked via non-reducible bonds.
authors.affiliation: Swiss Tropical Institute, Basel.
authors.forename: B
authors.initials: B
authors.lastname: Betschart
authors.forename: K
authors.initials: K
authors.lastname: Wyss
mesh_terms: D000818:Animals; D001200:Ascaris / Q000032:analysis*; D003094:Collagen / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D008854:Microscopy, Electron; D008970:Molecular Weight; D011487:Protein Conformation
chemical_list: D003094:Collagen