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
      Organic Chemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE