Biochemical characterization of the cuticle collagen of the nematode Caenorhabditis elegans.
Proteins of purified cuticles from adults of the small free-living nematode Caenorhabditis elegans are solubilized by reduction in the presence of a strong denaturing agent and then carboxymethylated. As in the large parasitic nematode Ascaris lumbricoïdes, these soluble proteins appeared to be collagens by their amino acid compositions. C. elegans cuticle collagen is separated into seven major components with different apparent molecular weights by molecular sieve chromatography and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The two main components, which together account for more than 64% of the total cuticle collagen, were extracted from gel after electrophoresis and analyzed. They differ in their amino acid compositions and would seem to represent genetically distinct collagen chains. The results presented lead to the hypothesis of the presence in this collagen of at least two different chains.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002107:Caenorhabditis / Q000032:analysis* / Q000648:ultrastructure; D002850:Chromatography, Gel; D003094:Collagen / Q000302:isolation & purification*; D008854:Microscopy, Electron; D008970:Molecular Weight; D011506:Proteins / Q000302:isolation & purification
D000596:Amino Acids; D011506:Proteins; D003094:Collagen