The isolation of human plasma prekallikrein
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چکیده
منابع مشابه
The isolation of human plasma prekallikrein.
1. The isolation of human plasma prekallikrein was achieved by fractionating human plasma on diethylaminoethyl cellulose (DEAE) in the presence of heparin.2. Heparin was shown to inhibit the activation of prekallikrein during the isolation procedure.3. The isolated prekallikrein fraction had some kallikrein activity which could be inhibited by diisopropylfluorophosphate (DFP) without affecting ...
متن کاملIsolation of high molecular weight activators of human plasma prekallikrein.
Two previously undescribed activators of prekallikrein have been purified from human plasma by alcohol frac tionation, ion exchange chromatography, gel filtration, and polyacrylamide gel electrophoresis. Both were apparently homogeneous as judged by electrophoretic mobility and molecular weight. A monomer-dimer relationship between these two activators is suggested by the use of disc gel electr...
متن کاملAutoactivation of human plasma prekallikrein.
Incubation of purified human plasma prekallikrein with sulfatides or dextran sulfate resulted in spontaneous activation of prekallikrein as judged by the appearance of amidolytic activity toward the chromogenic substrate H-D-Pro-Phe-Arg-p-nitroanilide. The time course of generation of amidolytic activity was sigmoidal with an apparent lag phase that was followed by a relatively rapid activation...
متن کاملPlasma Prekallikrein: Isolation, Characterization, and Mechanism of Activation
The precursor of the kinin-forming enzyme, prekallikrein, was isolated from rabbit plasma protected from activation during preparatory procedures. Prekallikrein was shown to be a 4.5S gamma(1)-glycoprotein with an isoelectric point of 5.9 and a mol wt of 99,900. The proenzyme was activated at neutral pH by an enzyme from rabbit or human plasma we have termed prekallikrein activator (PKA) or by ...
متن کاملRecombinant prolylcarboxypeptidase activates plasma prekallikrein.
The serine protease prolylcarboxypeptidase (PRCP), isolated from human umbilical vein endothelial cells (HUVECs), is a plasma prekallikrein (PK) activator. PRCP cDNA was cloned in pMT/BIP/V5-HIS-C, transfected into Schneider insect (S2) cells, and purified from serum-free media. Full-length recombinant PRCP (rPRCP) activates PK when bound to high-molecular-weight kininogen (HK). Recombinant PRC...
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ژورنال
عنوان ژورنال: British Journal of Pharmacology
سال: 1970
ISSN: 0007-1188
DOI: 10.1111/j.1476-5381.1970.tb10591.x