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Studies on Pharmacological Activation of Human Serum Immunoglobulin G by Chemical Modification and Active Subfragments. IX. Anti-inflammatory Activity of Completely Alkylated Heavy Chain (C.Fr.I-H)
The anti-inflammatory activity of completely reduced and carboxamide-methylated heavy chain of all disulfide bonds in human serum immunoglobulin G (IgG) (C.Fr.I-H) was investigated using some experimental inflammatory models. C.Fr.I-H significantly inhibited carrageenin-induced paw edema and pleuris...
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Published in: | Biological & pharmaceutical bulletin 1993/03/15, Vol.16(3), pp.309-311 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | The anti-inflammatory activity of completely reduced and carboxamide-methylated heavy chain of all disulfide bonds in human serum immunoglobulin G (IgG) (C.Fr.I-H) was investigated using some experimental inflammatory models. C.Fr.I-H significantly inhibited carrageenin-induced paw edema and pleurisy, and serotonin-induced paw edema. The carboxamide-methylated heavy chain of interchain disulfide bonds in IgG (Fr.I-H) exhibited similar inhibitory activities to C.Fr.I-H on carrageenin-induced paw edema and pleurisy, while it was ineffective on serotonin-induced paw edema. These results suggest that complete alkylation of disulfide bonds in a heavy chain caused stronger anti-inflammatory activities than partial alkylation. |
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ISSN: | 0918-6158 1347-5215 |
DOI: | 10.1248/bpb.16.309 |