Starch-Gel Electrophoretic Pattern of Pepsin-Treated Collagen.
- 1 January 1966
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 20 (5) , 1304-1308
- https://doi.org/10.3891/acta.chem.scand.20-1304
Abstract
When acetic acid-soluble rat-tail-tendon collagen was digested with pepsin, at first the [beta]-components and larger aggregates were broken down to [alpha]-components. In the second phase there were liberated at least seven distinct fragments, which yielded a reproducible starch-gel electrophoretic pattern. The effects of the various coditions during the digestion are described.This publication has 4 references indexed in Scilit:
- The cleavage of tyrosyl peptides by pepsin from collagen solubilised by the Nishihara techniqueBiochimica et Biophysica Acta (BBA) - General Subjects, 1965
- Effects of Pepsin Treatment on the Interaction Properties of Tropocollagen Macromolecules*Biochemistry, 1965
- Tropocollagen: Significance of Protease-Induced AlterationsScience, 1963
- The N-terminal amino acid residues of gelatin. 3. Enzymic degradationBiochemical Journal, 1955