scholarly journals Solubilization and Partial Characterization of Extensin Fragments from Cell Walls of Cotton Suspension Cultures (Evidence for a Covalent Cross-Link between Extensin and Pectin)

1995 ◽  
Vol 108 (4) ◽  
pp. 1691-1701 ◽  
Author(s):  
X. Qi ◽  
B. X. Behrens ◽  
P. R. West ◽  
A. J. Mort
Planta ◽  
2000 ◽  
Vol 211 (2) ◽  
pp. 256-264 ◽  
Author(s):  
Raynald Girault ◽  
Isabelle His ◽  
Christine Andeme-Onzighi ◽  
Azeddine Driouich ◽  
Claudine Morvan

1987 ◽  
Vol 244 (2) ◽  
pp. 303-309 ◽  
Author(s):  
K Barnard ◽  
N D Light ◽  
T J Sims ◽  
A J Bailey

The conversion of the reducible divalent cross-links in collagen to non-reducible multivalent cross-links in mature collagen has resulted in the identification of several new amino acids as the putative mature cross-link. None of these compounds has completely satisfied the necessary criteria. We have now isolated an amino acid of high Mr, derived from lysine, that is only present in high-Mr peptides derived from mature collagen. Its increase with age of the tissue correlates with the decrease in the reducible cross-links, and it is present both in mature skin and bone, which are initially cross-linked through the aldimine and oxo-imine divalent cross-link respectively. We propose that this amino acid, as yet incompletely characterized and designated compound M, is a major cross-link of mature collagen.


1983 ◽  
Vol 9 (5) ◽  
pp. 269-274 ◽  
Author(s):  
Hugo L. David ◽  
Nalin Rastogi

Sign in / Sign up

Export Citation Format

Share Document