title: Developmental changes in cuticular proteins of Ascaris suum.
abstract: 1. Cuticles were isolated from developmental stages of the swine nematode Ascaris suum by a combination of mechanical disruption and detergent treatment of larvae or by surgical removal of cuticle from adults. Proteins from the isolated cuticles were solubilized with 2-mercaptoethanol (2ME) and analyzed by SDS-PAGE. 2. 2ME soluble, cuticular proteins from adults consisted of 5 to 6 bands with 80% of proteins in 2 bands with mol. wts of 106,000 and 93,000. Cuticular proteins from the third and fourth larval stages (L3 and L4) were comparable to adult, but differences in the number of bands were observed. The soluble proteins from the adult, L3 and L4 were readily degraded by a bacterial collagenase suggesting that these proteins are collagen-like structural elements of the cuticle. 3. The soluble proteins from the second stage (L2) differed from the adult and other larval stages in both the number and mol. wt of protein bands and their lack of degradation by bacterial collagenase. Amino acid composition of soluble cuticular proteins were similar for adult and L4, but glycine and proline were present in lower amounts in the L2. 4. These results support a hypothesis that there are stage specific differences in cuticular proteins from A. suum and that the greatest differences appear to exist between L2 and other stages.
authors.affiliation: Helminthic Diseases Laboratory, USDA, BARC-East Beltsville, MD 20705.
authors.forename: R H
authors.initials: RH
authors.lastname: Fetterer
authors.forename: J F
authors.initials: JF
authors.lastname: Urban
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001200:Ascaris / Q000254:growth & development*; D004591:Electrophoresis, Polyacrylamide Gel; D007814:Larva; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis*
chemical_list: D000596:Amino Acids; D011506:Proteins