The isolation, purification, and characterization of the collagen of Cysticercus cellulosae.
Insoluble collagen fibrils were obtained from Cysticercus cellulosae after homogenization and treatment with NaCl/mercaptoethanol solutions and were solubilized after limited pepsin digestion. Solubilized Cysticercus collagen shows two different alpha subunits in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent molecular weight of 100,000 and is readily degraded by bacterial collagenase. The amino acid composition is characteristic of collagen except that it contains no hydroxyproline. Segment long spacing crystallites measuring 280 nm in length were prepared. These segments showed a band pattern different from that of vertebrate and other invertebrate collagens. The denaturation temperature at neutral pH was 35 degrees C and correlated with the total pyrrolidine content as observed for other collagens. An intrinsic viscosity value of 15.3 dl/g was obtained for this collagen. Its possible evolutionary relationship with other collagens is discussed.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003094:Collagen / Q000302:isolation & purification*; D003460:Crystallization; D003552:Cysticercus / Q000032:analysis*; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D011489:Protein Denaturation; D012867:Skin / Q000032:analysis; D013621:Taenia / Q000032:analysis*; D014783:Viscosity
D000596:Amino Acids; D010446:Peptide Fragments; D003094:Collagen