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Activation of the first component of complement, C1: comparison of the effect of sixteen different enzymes on serum C1
Authors:H P Heinz  M Loos
Affiliation:Institut für Medizinische Mikrobiologie der Johannes-Gutenberg-Universität Mainz, 6500 Mainz, Federal Republic of Germany
Abstract:In this study, the effect of sixteen different enzymes on serum C1 and its subcomponents was investigated. The sixteen enzymes could be divided into three groups. First, enzymes which activate native C1: trypsin (optimal concentration 2.4 x 10(-4) mM); alpha-chymotrypsin (2.3 x 10(3) mM); thrombin (1.0 x 10(-5) mM); plasmin (1.9 x 10(-5) mM); elastase (5.8 x 10(-5) mM); pronase (3.0 x 10(-6) mM). All these enzymes are serine esterase and activate native serum C1 bound to EAC4 at the given concentration within 10 min at 30 degrees C. Furthermore, native C1 inhibited by a pentosanpolysulfoester, Sp54, is unable to undergo the internal activation but can be externally activated by the serine esterases. Second, enzymes which do not activate native C1 but result in a dose and time-dependent loss of C1 activity: collagenase; pepsin; carboxypeptidase B. Third, enzymes which have no effect on C1 and C1: Lysozyme; neuraminidase; beta-galactosidase; L-amino acid oxidase; arginase; streptokinase, and acetylcholinesterase.
Keywords:Sheep erythrocytes (E) sensitized with rabbit IgG antibody (A) containing complement (C) components  ethylenediaminetetraacetate  veronal-buffered saline  veronal-buffered saline with sucrose
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