Antarctic Fish Immunoglobulins: Structure and Antibody Specificity
177
2C2.3, although lacking the main part of the leader, was shown to contain
the VH domain and the poly-A tail; in addition there might be a 3'
untranslated region. Sequencing of the entire C region is in progress.
D
pit
~
_ -75
-6 .0
~
_
- 21
· ~ . I
- 4 .7
- <1.4
Fig. 1. Purification of T bernacchii Ig. A: thiophilic adsorption chromatography on T-gel.
Arrow indicates the recovery of bound fraction. B: FPLC elution profile of T-gel bound
fraction. C: SDS-PAGE, under reducing conditions, of bile Ig (lane 1) and plasma Ig (lane
2). D: isoelectricfocusing (IEF) of plasma Ig
The molecular cloning approach will help extend our analysis of
Antarctic fish immunoglobulin structure by verifying: the VH region
diversity and the relationship to VH families from temperate teleost
species; the conservation of the domain structure in heavy chain; the
distribution of the cysteine residues involved in interchain and intersubunit
linkages; the conservation of the carbohydrate acceptor sites.