Abstract
We have used specific antibody probes to conserved antigenic motifs to identify and characterize immunoglobulin-related molecules in tunicates and a C-type lectin found in lamprey that is related to molecules found in tunicates and mammals. The tunicate immunoglobulin cross-reactive molecule (μCRM) reacts with antibodies raised to shark IgM heavy chains. Intact tunicate μCRM is a monomer of Ig light-chain-sized subunits and is oligoclonal by IEF. That this molecule is related to Ig is indicated both by immunochemical data and by peptide sequence homologies. The lamprey lectin is a large polymer (> 500,000 kDa) of 35-kDa and 60-kDa subunits. It appears to be related to C-type lectins as shown by peptide sequence homology and the requirement of Ca2+ for activity. Related molecules appear to be present in tunicates and mammals as shown by cross-reactivity of antibodies in Western blots with single bands from hemolymph and T-cell extracts.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 74-81 |
| Number of pages | 8 |
| Journal | Annals of the New York Academy of Sciences |
| Volume | 712 |
| State | Published - 1994 |
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ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
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Recognition molecules and immunoglobulin domains in invertebrates. / Schluter, S. F.; Schroeder, Joyce; Wang, E.; Marchalonis, J. J.
In: Annals of the New York Academy of Sciences, Vol. 712, 1994, p. 74-81.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Recognition molecules and immunoglobulin domains in invertebrates
AU - Schluter, S. F.
AU - Schroeder, Joyce
AU - Wang, E.
AU - Marchalonis, J. J.
PY - 1994
Y1 - 1994
N2 - We have used specific antibody probes to conserved antigenic motifs to identify and characterize immunoglobulin-related molecules in tunicates and a C-type lectin found in lamprey that is related to molecules found in tunicates and mammals. The tunicate immunoglobulin cross-reactive molecule (μCRM) reacts with antibodies raised to shark IgM heavy chains. Intact tunicate μCRM is a monomer of Ig light-chain-sized subunits and is oligoclonal by IEF. That this molecule is related to Ig is indicated both by immunochemical data and by peptide sequence homologies. The lamprey lectin is a large polymer (> 500,000 kDa) of 35-kDa and 60-kDa subunits. It appears to be related to C-type lectins as shown by peptide sequence homology and the requirement of Ca2+ for activity. Related molecules appear to be present in tunicates and mammals as shown by cross-reactivity of antibodies in Western blots with single bands from hemolymph and T-cell extracts.
AB - We have used specific antibody probes to conserved antigenic motifs to identify and characterize immunoglobulin-related molecules in tunicates and a C-type lectin found in lamprey that is related to molecules found in tunicates and mammals. The tunicate immunoglobulin cross-reactive molecule (μCRM) reacts with antibodies raised to shark IgM heavy chains. Intact tunicate μCRM is a monomer of Ig light-chain-sized subunits and is oligoclonal by IEF. That this molecule is related to Ig is indicated both by immunochemical data and by peptide sequence homologies. The lamprey lectin is a large polymer (> 500,000 kDa) of 35-kDa and 60-kDa subunits. It appears to be related to C-type lectins as shown by peptide sequence homology and the requirement of Ca2+ for activity. Related molecules appear to be present in tunicates and mammals as shown by cross-reactivity of antibodies in Western blots with single bands from hemolymph and T-cell extracts.
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UR - http://www.scopus.com/inward/citedby.url?scp=0028213859&partnerID=8YFLogxK
M3 - Article
C2 - 8192354
AN - SCOPUS:0028213859
VL - 712
SP - 74
EP - 81
JO - Annals of the New York Academy of Sciences
JF - Annals of the New York Academy of Sciences
SN - 0077-8923
ER -