The isolation and characterization of a mouse myeloma protein with anti-dextran activity
β Scribed by John H. Pazur; Michael E. Tay; Susan E. Rovnak; Beverly A. Pazur
- Publisher
- Elsevier Science
- Year
- 1982
- Tongue
- English
- Weight
- 545 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0165-2478
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Phytolacca anti-viral protein (PAP) was purified from Phytolacca leaves and the N-terminal was sequenced. A cDNA library was made from mRNAs isolated from Phytolacca leaves and cDNA clones for PAP were identified using oligonucleotide probes derived from the N-terminal amino acid sequence. The PAP-c
## Abstract Amino acid sequences have been determined for the first 26 residues at the amino (Nβ) terminus of the light chain, the first 27 residues of the heavy chain and the first 23 residues of a large heavy chain fragment of an IgG1 (ΞΊ) myeloma protein with antiβrubella specificity. These data
## Abstract This report describes studies carried out in an attempt to define the antibody specificity of a rabbit antiserum generated to the RPMI 8226 line of human myeloma cells and then isolate and characterize the antigen. The antiserum reacted to a significantly higher titer in a quantitative