| pubmed-article:3989305 | pubmed:abstractText | Pro-HNP, a urine protein isolated from hereditary nephritis patients, is derived from C3 and resembles the C3c domain. It contains disulfide-linked polypeptides of beta 75, alpha 40, and alpha 28. Plasmin degraded pro-HNP in vitro to HNP, which was also isolated from the urine of patients and which contained disulfide-linked polypeptides of beta 60, alpha 38, and alpha 26, and noncovalently bound polypeptide of beta 17. Amino terminal sequence analyses and amino acid compositions of the seven polypeptides isolated from pro-HNP and HNP show that beta 75 degrades to beta 60 and beta 17 (beta 17 locates at the amino end of beta 75), alpha 40 degrades to alpha 38 (both locate at the carboxyl end of the alpha-chain of C3), and alpha 28 degrades to alpha 26 (both are from the amino end of the alpha'-chain of C3b). These results confirm the enzymatic specificity of plasmin on pro-HNP. In HNP, the half-cystine contents of beta 60, alpha 38, alpha 26, and beta 17 were approximately 3, 12, 3, and 4, respectively. Partial reduction readily released alpha 40 from pro-HNP and alpha 38 from HNP. There were about five intra-chain disulfide bonds in alpha 40 or alpha 38; stepwise reduction of these intra-polypeptide bonds apparently accounted for multiple conformations of alpha 40 or alpha 38. | lld:pubmed |
