Activation of bovine factor XII (Hageman factor) by plasma kallikrein

Biochemistry ◽  
1980 ◽  
Vol 19 (7) ◽  
pp. 1322-1330 ◽  
Author(s):  
Kazuo Fujikawa ◽  
Ronald L. Heimark ◽  
Kotoku Kurachi ◽  
Earl W. Davie
Biochemistry ◽  
1977 ◽  
Vol 16 (10) ◽  
pp. 2270-2278 ◽  
Author(s):  
Kazuo Fujikawa ◽  
Kenneth A. Walsh ◽  
Earl W. Davie

1972 ◽  
Vol 28 (02) ◽  
pp. 169-181 ◽  
Author(s):  
H Gjønnæss

SummaryThe activating principle (CPA) of the factor VII activation seen in plasmas of women taking oral contraceptives after overnight incubation of the plasmas at 0° C was investigated. The reaction was dependent on low temperature, and factor XII was indispensable. Concomitant with the activation of factor VII a 10–30 fold increase in TAME esterolytic activity was observed together with a near 100 per cent drop in plasma kininogen concentration. The results indicated that the activation of factor VII is linked to activation of the kallikrein system, and that the activator may be plasma kallikrein.


1992 ◽  
Vol 67 (02) ◽  
pp. 219-225 ◽  
Author(s):  
Walter A Wuillemin ◽  
Miha Furlan ◽  
Hans Stricker ◽  
Bernhard Lämmle

SummaryThe plasma of a healthy woman was found to contain half normal factor XII (FXII) antigen level (0.46 U/ml) without any FXII clotting activity (<0.01 U/ml). The variant FXII in this plasma, denoted as FXII Locarno, was partially characterized by immunological and functional studies on the proposita’s plasma. FXII Locarno is a single chain molecule with the same size (M r = 80 kDa) as normal FXII. Isoelectric focusing suggested an excess of negative charge in the variant FXII as compared to normal FXII. In contrast to FXII in normal plasma, FXII Locarno was not proteolytically cleaved upon prolonged incubation of proposita’s plasma with dextran sulfate. Adsorption to kaolin was similar for both, abnormal and normal FXII. Incubation of the proposita’s plasma with dextran sulfate and exogenous plasma kallikrein showed normal cleavage of FXII Locarno outside of the tentative disulfide loop Cys340-Cys467, but only partial cleavage within this disulfide loop. Furthermore, plasma kallikrein-cleaved abnormal FXII showed neither amidolytic activity nor proteolytic activity against factor XI and plasma prekallikrein.These results suggest a structural alteration of FXII Locarno, affecting the plasma kallikrein cleavage site Arg353-Val354 and thus formation of activated FXII (a-FXIIa).


1977 ◽  
Vol 10 (2) ◽  
pp. 309-313 ◽  
Author(s):  
John Y.C. Chan ◽  
Clement E. Burrowes ◽  
Henry Z. Movat

Author(s):  
Liaqat Ali Chaudhry ◽  
Wael Yasin Mohamed El-Sadek ◽  
Ghazala Aslam Chaudhry ◽  
Feddha Eid Al-Atawi

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