Characterization of serum immunoglobulins in a chondrostean fish, Acipenser baeri.

Abstract:

:The euglobulin fraction of sturgeon (Acipenser baeri) serum was analyzed using electrophoretic and immunoblotting techniques. The major protein of this fraction is an IgM-like molecule composed of equimolar 70-kDa glycosylated H chains and 26-30 kDa L chains. In the absence of a reducing agent, the L and H polypeptides may form (mu 2L2)n high molecular weight polymers, mu 2L2 170-kDa units or L2 dimers. These different bonding patterns suggest some structural heterogeneity in the distribution of cysteine residues along the sturgeon Ig chains. The H chain N-terminal sequence indicates significant homologies with the conserved VHIII subgroup. Heavy chains antigenically different from the 70-kDa H chain were not detected, suggesting that IgM is the only Ig class synthesized by this sturgeon species.

journal_name

Dev Comp Immunol

authors

Partula S,Charlemagne J

doi

10.1016/s0145-305x(05)80007-2

subject

Has Abstract

pub_date

1993-11-01 00:00:00

pages

515-24

issue

6

eissn

0145-305X

issn

1879-0089

pii

S0145-305X(05)80007-2

journal_volume

17

pub_type

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