During the past year, the amino acid sequence of over 220 proteins and peptides has been determined by automated protein sequence analyses. In the case of several malaria proteins and a schistosome protein, the facility has purified tryptic peptides for sequence analysis by reverse phase microbore HPLC separation. Studies in which these analyses have had a major impact are listed below: (1) the characterization and identification of the putative gag- pol protease and gag encoded gene products of human immunodeficiency virus (HIV) (Laboratory of Molecular Microbiology); (2) the characterization of human pro-gastrin- release peptides expressed in baculovirus (Navy Medical Oncology Branch,778 NCI); (3) the identification of previously unidenitifed vaccinia virus encoded proteins (Laboratory of Viral Diseases); (4) the characterization of high-efficiency purified interleukin 4 (Laboratory of Immunology); (5) the structure of T-cell activating protein (TAP) and related Ly-6 encoded molecules (Harvard Medical School); (6) the identification of a chimeric MHC class II/class I protein expressed on the cell surface (Laboratory of Immunology); (7) protein sequence determinations which allowed the development of oligonucleotide probes for the cloning of PFs25 that is expressed on zygotes an ookinetics of P. falciparum (Laboratory of Parasitic Disease); (8) the identification of hamster MHC class I antigens (Laboratory of Immunopathology; (9) analysis of the BCDF (Il-6) receptor (Laboratory of Immunoregulation); (10) identification of Dengue virus pre-matrix structural protein (Laboratory of Infectious Disease).
