Abstract
Membrane-bound HLA-A and HLA-B antigens have been extensively purified in good yield. The sequences of the N-terminal 16 amino acids have been determined using about 1 nmol of protein eluted from polyacrylamide gel after electrophoresis in sodium dodecyl sulphate.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 200-205 |
| Number of pages | 6 |
| Journal | Nature |
| Volume | 261 |
| Issue number | 5557 |
| DOIs | |
| State | Published - Dec 1 1976 |
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All Science Journal Classification (ASJC) codes
- General
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Isolation and N-terminal amino acid sequence of membrane-bound human HLA-A and HLA-B antigens. / Bridgen, John; Snary, David; Crumpton, Michael J.; Barnstable, Colin; Goodfellow, Peter; Bodmer, Walter F.
In: Nature, Vol. 261, No. 5557, 01.12.1976, p. 200-205.Research output: Contribution to journal › Article
TY - JOUR
T1 - Isolation and N-terminal amino acid sequence of membrane-bound human HLA-A and HLA-B antigens
AU - Bridgen, John
AU - Snary, David
AU - Crumpton, Michael J.
AU - Barnstable, Colin
AU - Goodfellow, Peter
AU - Bodmer, Walter F.
PY - 1976/12/1
Y1 - 1976/12/1
N2 - Membrane-bound HLA-A and HLA-B antigens have been extensively purified in good yield. The sequences of the N-terminal 16 amino acids have been determined using about 1 nmol of protein eluted from polyacrylamide gel after electrophoresis in sodium dodecyl sulphate.
AB - Membrane-bound HLA-A and HLA-B antigens have been extensively purified in good yield. The sequences of the N-terminal 16 amino acids have been determined using about 1 nmol of protein eluted from polyacrylamide gel after electrophoresis in sodium dodecyl sulphate.
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UR - http://www.scopus.com/inward/citedby.url?scp=0017158410&partnerID=8YFLogxK
U2 - 10.1038/261200a0
DO - 10.1038/261200a0
M3 - Article
C2 - 1272392
AN - SCOPUS:0017158410
VL - 261
SP - 200
EP - 205
JO - Nature
JF - Nature
SN - 0028-0836
IS - 5557
ER -