Kinins IV pp 147-153 | Cite as

Reduced or Unchanged Cofactor Function of Human High Molecular Weight Kininogen Induced by Human Plasma Kallikrein

  • Harald Thidemann Johansen
  • Kjell Briseid
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 198A)


Plasma kallikrein activated spontaneously during the purification of prekallikrein (I) and acetone-activated plasma kallikrein (II) were at pH 7.4 both capable of reducing the capacity of purified human high molecular weight kininogen (HMrK) to function as cofactor in the contact phase activation of factor XII in a crude plasma preparation. At pH 6.8 only I had such an effect. SDS polyacrylamide gel electrophoresis with reduction indicated that both I and II contained kallikrein as a cleaved three-chain molecule. I contained in addition a Mr 49,000 fraction reflecting possibly uncleaved heavy chain. The registration of reduced cofactor function of HMrK induced by plasma kallikrein is discussed in view of the assay procedure used.


Cofactor Activity Plasma Kallikrein High Molecular Weight Kininogen Plasma Preparation Cofactor Function 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Harald Thidemann Johansen
    • 1
  • Kjell Briseid
    • 1
  1. 1.Department of Pharmacology, Institute of PharmacyUniversity University of Oslo, BlindernOslo 3Norway

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