Loading…

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...

Full description

Saved in:
Bibliographic Details
Published in:Biological & pharmaceutical bulletin 1993/03/15, Vol.16(3), pp.309-311
Main Authors: MIMURA, Tsutomu, ITOH, Masaaki, HARUYAMA, Munetada, SUGIYAMA, Tetsuya, SUZUKI, Nobutaka, TSUJIKAWA, Kazutake, KOHAMA, Yasuhiro
Format: Article
Language:English
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
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.
ISSN:0918-6158
1347-5215
DOI:10.1248/bpb.16.309