Molecular Recognition of Alpha-Neurotoxins
Abstract
Synthesis, purification and characterization of the human AcChoR alpha-chain peptides have been reported (10). The alpha-neurotoxin binding regions on human AcChoR reside in the peptides shown in Fig. 1. These peptides were employed in the present work. The receptor-binding regions on Bgt are present in the three loop peptides. The synthesis, purification and characterization of the monomeric forms of the three cyclic peptides(Fig. 1.) have been described. Bgt and its synthetic peptides were labeled with iodine-125 using the chloramine-T method. Radioiodinated materials were used immediately after labeling. The specific activities of the labeled peptides were: LIN,3. 1x103 cpm/p mole; L2, 2.4x103cpm/p mole; L3E, 2.1x103cpm/p mole. The coupling of proteins and peptides to CNBr-activated Sepharose CL-4B was carried out under optimum conditions as described previously. The binding of I-labeled Bgt or Bgt peptides to adsorbents of the human AcChoR peptides was determined by a quantitative solid-phase radiometric binding assay.
Document Details
- Document Type
- Technical Report
- Publication Date
- Nov 30, 1990
- Accession Number
- ADA230342
Entities
People
- Zouhair M. Atassi
Organizations
- Baylor College of Medicine