New and rapid functional assay for C1 inhibitor in human plasma
نویسندگان
چکیده
منابع مشابه
New and rapid functional assay for C1 inhibitor in human plasma.
C1 inhibitor (C1-INH) and alpha 2-macroglobulin (alpha 2M) account for over 90% of the inactivation of purified plasma kallikrein by normal human plasma. The rate of kallikrein inactivation is also dependent on the presence of high molecular weight kininogen (HMWK), which forms a reversible complex with kallikrein protecting the active site of the enzyme against inhibitors. By selectively inact...
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c i’ inhibitor (Ci-INH) and a2-macroglobulin (a2M) account for over 90% of the inactivation of purified plasma kallikrein by normal human plasma. The rate of kallikrein inactivation is also dependent on the presence of high molecular weight kininogen (HMWK). which forms a reversible complex with kallikrein protecting the active site of the enzyme against inhibitors. By selectively mactivating a...
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We present a new functional assay for the first complement component (C1) in plasma, based on its activation by inhibition of the C1-esterase inhibitor (C1-inh) when monospecific antiserum to C1-inh is added to the plasma. After maximal activation, we can determine the concentration of activated C1 by using an amidolytic rate assay with a chromogenic substrate. We have optimized the assay condi...
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C1- inhibitor (C1(-)-Inh) catabolism in plasma of patients with hereditary angioneurotic edema (HANE) was assessed by measuring the complexes formed by C1(-)-Inh with its target proteases (C1-s, Factor XIIa, and kallikrein) and a modified (cleaved) inactive form of C1(-)-Inh (iC1(-)-Inh). This study was performed in plasma from 18 healthy subjects and 30 patients with HANE in remission: 20 with...
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ژورنال
عنوان ژورنال: Blood
سال: 1982
ISSN: 0006-4971,1528-0020
DOI: 10.1182/blood.v59.4.719.bloodjournal594719