Collagen heterogeneity in normal rabbit cornea. I. Isolation and biochemical characterization of the genetically-distinct collagens.
Limited proteolysis of preparations of mature rabbit cornea with pepsin allows the recovery of approximately 90% of the tissue collagen in soluble form. Using recently described selective precipitation techniques, the soluble cornea collagen can be resolved into two major fractions. The predominant fraction, which accounts for about 95% of the solubilized collagen, was identified by means of solubility properties, electrophoretic and chromatographic properties, as well as amino acid analyses of its constituent chains, as Type I collagen. The alternate fraction, which accounts for virtually all of the remainder of the solubilized cornea collagen, was identified by means of the same criteria as collagen comprised of the A and B chains. In addition, the stoichiometry of the latter chains in preparations of cornea collagen indicate that in the cornea these chains are likely to participate in the formation of only one type of collagen molecule with the chain composition, AB2. And finally, the demonstration that Type I and the AB2 collagens are the predominant forms of collagen recoverable from the mature cornea strongly suggests that molecules comprised of the A and B chains are not necessarily confined to basement membrane structures.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000032:analysis / Q000235:genetics / Q000302:isolation & purification*; D003315:Cornea / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D011817:Rabbits
D000596:Amino Acids; D003094:Collagen