Abstract
Purified human plasma kininogen of mol. wt 70,000 has been shown to be resistant to carboxypeptidase B treatment and to be a substrate for both plasma and urinary kallikrein. Two kininogen-containing peaks isolated from fresh plasma by stepwise column Chromatography on Sephadex DEAE-A50 were shown to have identical mobility upon disc gel electrophoresis in 8 M urea or after neuraminidase treatment and to have sedimentation coefficients slightly smaller and slightly larger than that of albumin. These data, together with a difference in partial specific volume, suggest a role for carbohydrate content in accounting for the apparent heterogeneity of kininogens.
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