Antibodies to chick-tendon procollagen. Affinity purification with the isolated disulfide-linded NH2-terminal extensions and reactivity with a component in embryonic serum.
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Antisera were prepared by immunizing a rabbit with procollagen synthesized and secreted by cells from chick embryo tendons. Specific antibodies were then purified from the antisera by using an immunoadsorbent which contained the isolated NH2terminal extensions of procollagen. The purified antibodies were shown to react specifically with intact procollagen as well as with procollagen in which the interchain disulfide bonds were ruptured by reduction under nondenaturing conditions. The antibodies also reacted with the pro1 chain but not the pro2 chain isolated from the procollagen. There was no reaction after the intrachain bonds in the pro chains of the procollagen were reduced under denaturing conditions and alkylated. In the course of characterizing the antibodies it was shown that the NH2terminal extensions on the two pro1 chains and the one pro2 chain of type I procollagen are nonidentical. Also, it was shown that the serum of chick embryos contains an antigen which reacts with the specific antibodies to procollagen. Copyright 1974, Wiley Blackwell. All rights reserved
