Abstract
A method for the separation of collagen chains has been developed by employing two-dimensional gel electrophoresis which consists of isoelectric focusing in a 4% polyacrylamide gel-6 M urea-2% Pharmalyte with a pH gradient ranging 7 to 10 in the first dimension and SDS-polyacrylamide slab gel (5%, plus 3 M urea) electrophoresis in the second dimension. The method gives reproducible results and can be employed for the separation of α-chains of types I, II, III and V (AB) collagens as low as 10 ψg and for the estimation of their isoelectric points. Apparent isoelectric points of α1(I), α2, α1(II), α1(III), αA and αB-chains of bovine collagens were found to be 8.8, 9.2, 8.7, 9.1, 8.6 and 8.3 respectively.
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