作者: S S Huang , P O'Grady , J S Huang
DOI: 10.1016/S0021-9258(19)57337-9
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摘要: 125I-Labeled human platelet-derived transforming growth factor beta (125I-TGF-beta) and alpha 2-macroglobulin (alpha 2M) formed a complex as demonstrated by 5% native polyacrylamide gel electrophoresis. The 125I-TGF-beta.alpha 2M migrated at position identical to that of the fast migrating form 2M. Most could be dissociated acid or urea treatment. When 125I-TGF-beta was incubated with serum, high molecular weight immunoprecipitated anti-human anti-sera sodium dodecyl sulfate-polyacrylamide purified from platelet-rich plasma also showed latent activity immunoreactivity TGF-beta. These results suggest TGF-beta.alpha is