Premium
Collagen crosslinking: Isolation of a dimeric crosslinked peptide of α1‐CB6 from bovine corneal and scleral collagens
Author(s) -
Harding John J.,
Crabbe M.James C.
Publication year - 1979
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(79)80367-1
Subject(s) - ophthalmology , chemistry , art , polymer science , microbiology and biotechnology , art history , medicine , biology
The pattern of CNBr fragments of various collagens on SDS-polyacrylamide electrophoresis gels includes a major band with mobility intermediate between a2-CB(3-5) and a2-CB4 which has been called (Al-CB(3-7) and cxl-CB(S-8-3) on the basis of molecular weights from the gels [ 1,2]. We have noted a similar component which we will call component X, in gel patterns of CNBr fragments from unreduced corneal collagen [3], reduced cornea1 collagen and reduced scleral collagen. Our CNBr digestion conditions are harsher than those most used and we find no methionine in the digest; also we have not isolated any uncleaved fragments [3], so its seems unlikely that this major component could be an uncleaved peptide as has been suggested. Furthermore oil-CB3, part of both the proposed uncleaved peptides, is readily isolated in high yield (<60%) from CNBr digests of both cornea1 and scleral collagen (J .J.H., N. A. Panjwani, M.J.C.C., unpublished results). In the present work we have isolated component X from CNBr digests of cornea1 and scleral collagen and identified it as a dimer of al-CB6.