Isolation of the alpha 3-chain of human type V collagen and characterization by partial sequencing.
The alpha 1 alpha 2 alpha 3-chain form of human type V collagen was solubilized from placenta by pepsin treatment and isolated by ion-exchange chromatography. The alpha 3-chain was further separated after denaturation of the triple helix also by ion-exchange chromatography, cleaved with lysyl endopeptidase and the fragments separated by size-exclusion chromatography and reversed phase HPLC. N-Terminal sequence analysis of the fragments and comparison to sequences contained in a database indicated a relatively high similarity of the alpha 3(V)-chain to alpha 1(V) and alpha 1(XI) with an identity of approximately 73%.
Mann
K
K
Max-Planck-Institut für Biochemie, Martinsried, Germany.
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000737:chemistry* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010434:Pepsin A; D010446:Peptide Fragments / Q000302:isolation & purification; D010920:Placenta / Q000737:chemistry*; D011247:Pregnancy; D012689:Sequence Homology, Nucleic Acid; D014714:Vertebrates
D046911:Macromolecular Substances; D010446:Peptide Fragments; D003094:Collagen; D010434:Pepsin A