Title : Amino acid
sequence of the carboxyl-terminal hydrophilic
region of the H-2Kb MHC alloantigen
Abstract :
- Completion of the entire primary structure of the H-2Kb molecule
- The amino acid sequence of the COOH-terminal hydrophilic region of the H-2Kb histocompatibility antigen was determined
- The sequence was completed by analyses of four CNBr fragments obtained from the intact molecule as well as tryptic peptides
- This region was composed of 39 amino acid residues with a cluster of basic residues at the NH2 terminus and localized positions 308-346 of the H-2Kb molecule
- These sequence data, together with those reported for the NH2-terminal 284 residues [Martinko, J. M., Uehara, H. , Ewenstein , B. M., Kindt, T. J., Coligan, J. E., & Nathenson, S. G. (1980) Biochemistry 19, 6188-6193] and for the intramembranous segment [Uehara, H., Coligan, J. E., & Nathenson, S. G. (1981) Biochemistry (preceding paper in this issue)], provided the complete primary structure of the H-2Kb molecule
- This is the first histocompatibility antigen for which the entire primary structure is determined