Locust collagen: morphological and biochemical characterization.
Segment-long-spacing crystallites and reconstituted fibrils have been made from collagen extracted from the ejaculatory duct of the adult male locust, Locusta migratoria. These show the same banding pattern after positive staining as segment-long-spacing crystallites and fibrils made from mammalian type I collagen. Native fibrils show the same periodic pattern as type I fibrils, but it is not so distinct. Biochemical analysis of pepsin-digested locust collagen shows that there are two collagenous components. The alpha chains of the major component are similar to mammalian alpha 1 (I) chains, except that the number of hydroxylysine residues is elevated and the CNBr peptides differ. There are no alpha 2 chains; hence this locust collagen molecule is an alpha 1 trimer. The second component, which is present in only minute quantities, may be a type IV basement membrane collagen. It is concluded that the fibrous collagen molecule of the locust is very similar to that of mammalian type I trimers and to those of other invertebrates which have been examined.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003094:Collagen / Q000302:isolation & purification*; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D006110:Grasshoppers / Q000378:metabolism*; D008297:Male; D008854:Microscopy, Electron; D010434:Pepsin A; D010446:Peptide Fragments / Q000032:analysis; D012967:Sodium Dodecyl Sulfate
D000596:Amino Acids; D010446:Peptide Fragments; D012967:Sodium Dodecyl Sulfate; D003094:Collagen; D010434:Pepsin A; D003488:Cyanogen Bromide