| Objective: To prepare a specific immunoadsorbent for pathogenicacetylcholine receptor antibodies (AChRAb) in myasthenia gravis (MG). Theadsorptive mechanism and blood compatibility character of adsorbent werestudied by whole blood perfusion experiment. Methods: The cellulose beadswere prepared as carriers. A 10 synthesized amino acids of main immunogenicregion of human AChR or L-tryptophan, as ligands were immobilized oncellulose beads to make immunoadsorbents respectively. In this experiment thenormal 12 rabbits were randomly divided into three groups, including controlgroup (group A, only cellulose beads), L-tryptophan group (group B) andspecific group (group C). Blood cells, ions and plasma proteins were examinedbefore and after experiment, t test was applied in analysis of the data. Results:There was no significant difference in group A in blood cells, ions and proteinsbefore and after experiment. There were non-significant differences betweengroup B and group C in blood cells and in ions, but it was significant decreasedin plasma proteins in group B and in group C. Plasma total proteins (TP) were60.50±7.68 and 51.00±9.42 (P＜0.05), Plasma globulins (Glo) were 24.25±4.57 and 19.50±6.40 (P＜0.05) and plasma albumin (Alb) were 36.25±3.30 and31.50±3.70 (P＜0.05) respectively in group B. TP were 57.50±2.52 and 46.50±3.32 (P＜0.05), Glo were 23.75±1.89 and 16.75±2.36 (P＜0.05) and Albwere 33.75±2.63 and 29.50±1.91 (P＜0.05) respectively in group C. Theplasma proteins were significantly lower in group B and C than those in group A.Conclusion: The whole blood perfusion experiment was not destructive in rabbit blood examination. Blood cells and ions were not changed obviously in specificimmunoadsorbent group, but plasma proteins were decreased. This function wassimilar to L-tryptophan as ligand. The specific immunoadsorbent was favorablein blood compatibility character and it can be adapted to treat MG.
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