Isolation and partial characterization of cuticular collagen from the parasitic nematode Gaigeria pachyscelis.

The cuticle from adult Gaigeria pachyscelis was isolated by solubilizing the internal tissues with sodium dodecyl sulphate (SDS) at 37 degrees C. Cuticular protein was extracted with guanidine-HCl and beta-mercaptoethanol and purified by ammonium sulphate fractionation and DEAE-cellulose chromatography. SDS-polyacrylamide gel electrophoresis of purified protein revealed 2 polypeptides with apparent mol. wts of 58,000 and 74,000. As judged from their hydroxyproline content both of them are collagenous in nature. Results of gel filtration indicate that cuticular collagen exists in two forms, a non-associated form at low concentration and an associated form at high concentration.