Accession Number : ADA298304
Title : Isolation and Preliminary Characterization of a Recombinant TAT Protein From Human Immunodeficiency Virus.
Descriptive Note : Annual rept. 24 May 94-23 May 95,
Corporate Author : MORGAN STATE UNIV BALTIMORE MD
Personal Author(s) : Walls, Lichun H.
PDF Url : ADA298304
Report Date : 23 MAY 1995
Pagination or Media Count : 17
Abstract : Human immunodeficiency virus type-1 (HIV-1) Tat protein is a transactivator of viral gene expression. Tat as an over-expressed fusion protein, Rop-Tat has been purified after cyanogen bromide cleavage by using S-Sepharose Q-Sepharose column chromatography and subsequent use of HPLC. It is about 90% pure and the major impurity is a peptide which is 4 amino acids shorter than Tat, caused by breaking the acid labile bond of aspartate-proline under the acidic cleavage condition of cyanogen bromide. The fusion protein, Rop-Tat was purified by using the same procedures used for Tat. The next step will be refolding of Tat and Rop-Tat.
Descriptors : *PROTEINS, *VIRUSES, *HUMAN IMMUNODEFICIENCY VIRUSES, *BROMIDES, PEPTIDES, ISOLATION, IMPURITIES, GENES, MEDICAL SERVICES, MEDICAL RESEARCH, AMINO ACIDS, VIRAL PNEUMONIA, HOSTS(BIOLOGY), CLEAVAGE, CYANOGEN.
Subject Categories : Medicine and Medical Research
Distribution Statement : APPROVED FOR PUBLIC RELEASE