Isolation and Preliminary Characterization of a Recombinant TAT Protein From Human Immunodeficiency Virus.

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.

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Document Details

Document Type
Technical Report
Publication Date
May 23, 1995
Accession Number
ADA298304

Entities

People

  • Lichun H. Walls

Organizations

  • Morgan State University

Tags

DTIC Thesaurus Topics

  • Acids
  • Amino Acids
  • Chemistry
  • Chromatography
  • Column Chromatography
  • Cyanides
  • Electrophoresis
  • Gel Electrophoresis
  • Hiv Infections
  • Laboratory Animals
  • Materials
  • Molecular Weight
  • Molecules
  • Nitrogen Compounds
  • Polysaccharides
  • Recombinant Dna
  • Standards

Fields of Study

  • Biology

Readers

  • Immunology
  • Organic Chemistry