| Original language | English (US) |
|---|---|
| Pages (from-to) | S76 |
| Journal | Developmental and Comparative Immunology |
| Volume | 15 |
| Issue number | SUPPL. 1 |
| DOIs | |
| State | Published - 1991 |
ASJC Scopus subject areas
- Immunology
- Developmental Biology
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In: Developmental and Comparative Immunology, Vol. 15, No. SUPPL. 1, 1991, p. S76.
Research output: Contribution to journal › Article › peer-review
}
TY - JOUR
T1 - Isolation of a putative protoimmunoglobulin in Pyura hausteria
AU - Schroeder, J. A.
AU - Schluter, Samuel F.
AU - Marchalonis, John J.
N1 - Funding Information: ISOLATION OF A PUTATIVE PROTOIMMUNOGLOBULIN IN PYURA HAIJ~TERIA *J.A.Schroeder, Samuel F. Schluter, and John J. Marchalonis. Department of Microbiology and Immunology, University of Arizona, Tucson AZ 85724 The tunicate Pyura hausteria is a sessile marine protochordate which represents an advanced example of the phylum. All tunicates also display, at some point in their life, three early developmental characteristics that are physically distinctive of the phylum Chordata. Due to this link between the protochordates and chordates, it is possible that tunicates may share the portion of the chordate gene pool that codes for the rearranging mechanism of the immunoglobulin superfamily. The cyclostome lamprey, which is an example of the most primitive of the vertebrates, was used in all serological reactions with Pyura - surmising that lamprey immunoglobulin proteins would show a conservation of possible protoirrununoglobulin molecule exhibited in the tunicates. Using antibodies against the lamprey immunoglobulin in cross-reaction tests with the tunicate hemolymph, we have detected a protein of 28kDa which reacts with the lamprey immunoglobulin heavy chain. Through working with the Pyura hemolymph, we have developed a purification method for this 28kDa protein. This method will be used to purify high quantities of the tunicate hemolymph and the resultant protein will be sequenced. This final sequencing will determine the actual degree of homology between the tunicate protein and vertebrate immunoglobulin chains. We believe that much can be learned about the evolution of the chordate adaptive immune system through the study of these immunoglobulin-reactivep roteins of the protochordates. Supported in part by NSF grant # DCB8802353 JJM (PI) and NIH grant # GM42437 JJM (PI).
PY - 1991
Y1 - 1991
UR - http://www.scopus.com/inward/record.url?scp=27244462835&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=27244462835&partnerID=8YFLogxK
U2 - 10.1016/0145-305X(91)90282-4
DO - 10.1016/0145-305X(91)90282-4
M3 - Article
AN - SCOPUS:27244462835
SN - 0145-305X
VL - 15
SP - S76
JO - Developmental and Comparative Immunology
JF - Developmental and Comparative Immunology
IS - SUPPL. 1
ER -