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JJ Houle, EM Hoffmann and AF Esser
Department of Comparative & Experimental Pathology, University of
Florida, Gainesville.
The hemolytic efficiency and binding of C9 to homologous and heterologous
erythrocytes was evaluated by using a standardized passive sensitization
procedure to prepare antigen- and antibody-coated erythrocytes (EA) and
human serum for lysis. Heterologous bovine EA were readily lysed by human
serum, whereas human EA were quite resistant to lysis. Human EA bound as
many C8 and C9 molecules per cell as bovine EA when incubated under
identical conditions, but four times as much bound C9 was required to lyse
an equal number of human EA compared with bovine EA. The susceptibility of
human erythrocytes did not increase when increased volumes of undiluted
human serum were used although C9 binding increased to as much as 100,000
molecules per cell. Sodium dodecyl sulfate-resistant polymerized C9
(poly(C9)) was detected on both lysed ghosts and unlysed EA bearing
complement proteins C1 through C9 (EAC1-9) after incubation with undiluted
human serum; however, the ratio of poly(C9) to monomeric C9 was higher on
unlysed cells than on ghosts. Although bovine and human EA bound equal
amounts of human C9 at the end point, the rate of lysis and C9 uptake was
slower on homologous cells. The rate-limiting step occurred before C9
binding and lysis because the rates of lysis and C9 binding were equal on
homologous and heterologous EAC1-8 targets, but the extent of lysis of
homologous cells was still lower than lysis of heterologous cells. Human
erythrocytes lose restriction against homologous hemolysis during storage
in autologous plasma or in isotonic buffers.
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| Copyright © 1988 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
