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Effect of Calcium and Factor D Depletion on C3 Conversion by Rat Intestinal Glycoprotein
Author(s) -
WINSNES R.
Publication year - 1979
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1979.tb02715.x
Subject(s) - alternative complement pathway , glycoprotein , zymosan , classical complement pathway , calcium , chemistry , complement system , complement (music) , biochemistry , medicine , endocrinology , biology , immunology , in vitro , antibody , organic chemistry , complementation , gene , phenotype
These studies demonstrate that a rat intestinal glycoprotein fraction may activate C3 in normal human serum by the alternative complement pathway alone and by the classical pathway alone. Conversion of C3 by the rat intestinal glycoprotein fraction amounted to 55% when both the classical and the alternative pathways were intact, to 21% when the classical pathway was blocked by ethyleneglycol‐bis‐(β‐aminoethyl ether)N,N′‐tetraacetic acid, and to 21% in Factor‐D‐depleted serum. Comparable figures for zymosan were 58% 44% and 12%, and for sheep erythrocytes sensitized with anti‐sheep haemolysin, 27%, <1% and 21% respectively.