Extraction, isolation and characterization of neutral salt soluble type V collagen from fetal calf skin.
Collagen was extracted with neutral salt solution and examined for the presence of type V collagen. A fraction which was insoluble in both 0.02 M Na2HPO4, pH 9.2 and phosphate-buffered saline (PBS) pH 7.2 at 4 degrees C contained both alpha 1(V)- and alpha 2(V)-chains demonstrated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, diethylaminoethyl cellulose ion exchange chromatography, amino acid analysis and segment long spacing (SLS) crystallites. SLS crystallites showed a globular N-terminal extension peptide attached to the type V collagen monomer. Ion exchange chromatography also demonstrated the presence of a third, minor component, which was identified as the alpha 3(V)-chain. In certain extractions, components corresponding to the partially processed procollagen chains of type V collagen were also observed.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D003094:Collagen / Q000145:classification / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000032:analysis; D008854:Microscopy, Electron; D010084:Oxidation-Reduction; D010434:Pepsin A; D011347:Procollagen / Q000302:isolation & purification; D012867:Skin / Q000032:analysis* / Q000196:embryology
D000596:Amino Acids; D006023:Glycoproteins; D011347:Procollagen; D003094:Collagen; D010434:Pepsin A