Summary
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.
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© 1986 Plenum Press, New York
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Johansen, H.T., Briseid, K. (1986). Reduced or Unchanged Cofactor Function of Human High Molecular Weight Kininogen Induced by Human Plasma Kallikrein. In: Greenbaum, L.M., Margolius, H.S. (eds) Kinins IV. Advances in Experimental Medicine and Biology, vol 198A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5143-6_20
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DOI: https://doi.org/10.1007/978-1-4684-5143-6_20
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