Abstract
Five monoclonal anti-alpha-fetoprotein (AFP) antibodies (IgG1) were isolated from six fusions. They were characterized by examining titration values, affinity constants, isotypes, and epitope binding. Employing an epitope-blocking procedure which was based on the exclusion of like antibodies, four of the five monoclonal antibodies were found to be different. Antibody individuality was further demonstrated by comparison of isoelectric focusing patterns. The existence of four distinct anti-AFP antibodies strongly suggests the presence of at least that many epitopes on the AFP molecule.
| Original language | English |
|---|---|
| Pages (from-to) | 177-185 |
| Number of pages | 9 |
| Journal | Hybridoma |
| Volume | 3 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1984 Jan 1 |
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All Science Journal Classification (ASJC) codes
- Immunology
- Genetics
Cite this
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Characteristics of five monoclonal anti-alpha-fetoprotein antibodies. / Wellerson, R.; Shaw, Shyh-Yu; Kaplan, P.
In: Hybridoma, Vol. 3, No. 2, 01.01.1984, p. 177-185.Research output: Contribution to journal › Article
TY - JOUR
T1 - Characteristics of five monoclonal anti-alpha-fetoprotein antibodies
AU - Wellerson, R.
AU - Shaw, Shyh-Yu
AU - Kaplan, P.
PY - 1984/1/1
Y1 - 1984/1/1
N2 - Five monoclonal anti-alpha-fetoprotein (AFP) antibodies (IgG1) were isolated from six fusions. They were characterized by examining titration values, affinity constants, isotypes, and epitope binding. Employing an epitope-blocking procedure which was based on the exclusion of like antibodies, four of the five monoclonal antibodies were found to be different. Antibody individuality was further demonstrated by comparison of isoelectric focusing patterns. The existence of four distinct anti-AFP antibodies strongly suggests the presence of at least that many epitopes on the AFP molecule.
AB - Five monoclonal anti-alpha-fetoprotein (AFP) antibodies (IgG1) were isolated from six fusions. They were characterized by examining titration values, affinity constants, isotypes, and epitope binding. Employing an epitope-blocking procedure which was based on the exclusion of like antibodies, four of the five monoclonal antibodies were found to be different. Antibody individuality was further demonstrated by comparison of isoelectric focusing patterns. The existence of four distinct anti-AFP antibodies strongly suggests the presence of at least that many epitopes on the AFP molecule.
UR - http://www.scopus.com/inward/record.url?scp=0021636796&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021636796&partnerID=8YFLogxK
U2 - 10.1089/hyb.1984.3.177
DO - 10.1089/hyb.1984.3.177
M3 - Article
VL - 3
SP - 177
EP - 185
JO - Monoclonal Antibodies in Immunodiagnosis and Immunotherapy
JF - Monoclonal Antibodies in Immunodiagnosis and Immunotherapy
SN - 2167-9436
IS - 2
ER -