Abstract:
:The major product of digestion of bovine IgG2a(A1) with immobilized pepsin is F(ab')2 while similar treatment of IgG2a(A2) yields Fab, Fc and other products. It is postulated that structural differences in the hinge region, including the absence of the most N-terminal disulfide bridge in IgG2a(A2) and a displacement of the primary pepsin cleavage site toward the Fd, can explain this effect. The immunodominant A1 allotope(s) appears to be located in the CH3 domain of IgG2a(A1) while the A2 allotopes are located elsewhere and are apparently affected by digestion. The allotypic bias of rabbit anti-IgG2a is also present in anti-IgG2a raised in goats. However, the A2 allotypic determinants of bovine IgG2a are recognized by goat precipitins although precipitins of this specificity are not detectable in rabbits immunized with IgG2a(A2). Rabbit anti-A2 antibodies are detectable using the ELISA in rabbits immunized with IgG2a(A2).
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Heyermann H,Butler JEdoi
10.1016/0161-5890(87)90128-3subject
Has Abstractpub_date
1987-12-01 00:00:00pages
1327-34issue
12eissn
0161-5890issn
1872-9142journal_volume
24pub_type
杂志文章abstract::Increasing lines of evidence indicate that arsenic may be associated with immune related problems, but its detailed effects on immune organs are poorly understood. The objective of this study was to explore inflammatory responses and T cell differentiation of arsenic exposure in spleen and thymus. Female C57BL/6 mice ...
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journal_title:Molecular immunology
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pub_type: 杂志文章
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pub_type: 杂志文章
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