Abstract
Chromatographic separation by Sephadex G 200 of a crude kininogen fraction from intact, glass-treated or diluted and subsequently urokinase-activated human plasma shows the existence of two functionally different kininogens. The high molecular weight kininogen = kininogen II (apparent MW 110,000) is consumed by contact treatment; on the other hand, generation of plasmin leads to the disappearance of the low molecular weight kininogen = kininogen I. Both substrates are preformed in plasma. Trypsin and pancreatic kallikrein likewise form kinin from both substrates, while contact-activated kininogenase = kininogenase II preferably attacks kininogen II. These results are direct evidence for the existence of two kinin-forming systems in human plasma.
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