Abstract
The complete covalent structure has been determined for a human myeloma IgA1 immunoglobulin. This protein has unique features in the amino acid sequence and disulfide bridge structure of the variable (V) and constant (C) regions of both the α heavy and the λ light chains, and in the number and loci of oligosaccharides. Whereas C region domains of heavy chains have evolved independently over eons, recent isotypic variations have occurred in λ light chains and possibly in a heavy chains.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1017-1020 |
| Number of pages | 4 |
| Journal | Science |
| Volume | 193 |
| Issue number | 4257 |
| State | Published - 1976 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- General
Cite this
Complete covalent structure of a human IgA1 immunoglobulin. / Liu, Yu Sheng Victor; Low, Teresa L K; Infante, Anthony J; Putnam, Frank W.
In: Science, Vol. 193, No. 4257, 1976, p. 1017-1020.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Complete covalent structure of a human IgA1 immunoglobulin
AU - Liu, Yu Sheng Victor
AU - Low, Teresa L K
AU - Infante, Anthony J
AU - Putnam, Frank W.
PY - 1976
Y1 - 1976
N2 - The complete covalent structure has been determined for a human myeloma IgA1 immunoglobulin. This protein has unique features in the amino acid sequence and disulfide bridge structure of the variable (V) and constant (C) regions of both the α heavy and the λ light chains, and in the number and loci of oligosaccharides. Whereas C region domains of heavy chains have evolved independently over eons, recent isotypic variations have occurred in λ light chains and possibly in a heavy chains.
AB - The complete covalent structure has been determined for a human myeloma IgA1 immunoglobulin. This protein has unique features in the amino acid sequence and disulfide bridge structure of the variable (V) and constant (C) regions of both the α heavy and the λ light chains, and in the number and loci of oligosaccharides. Whereas C region domains of heavy chains have evolved independently over eons, recent isotypic variations have occurred in λ light chains and possibly in a heavy chains.
UR - http://www.scopus.com/inward/record.url?scp=0017160906&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017160906&partnerID=8YFLogxK
M3 - Article
C2 - 821146
AN - SCOPUS:0017160906
VL - 193
SP - 1017
EP - 1020
JO - Science
JF - Science
SN - 0036-8075
IS - 4257
ER -