Document Detail


Expression and characterization of the reverse transcriptase enzyme from type 1 human immunodeficiency virus using different baculoviral vector systems.
MedLine Citation:
PMID:  8575439     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
To produce the human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) in amounts required to study its structure and function, the p66 enzyme subunit was expressed using two different baculovirus vectors in Sf158 insect host cells. Both vectors permitted an efficient HIV-1 RT expression. The resulting products were purified up to 90% homogeneity, characterized, and investigated for their susceptibility to digestion with various proteases. The recombinant baculoviral RT obtained with the pAc373 expression vector was purified as a p66/p60 heterodimer. The recombinant His-RT was expressed with the pBlueBacHis vector. Thereby, the protein was tagged with an N-terminal hexahistidine peptide and it was purified as a p70/p70 homodimer. The two enzymes differed in their specific activity, kinetic properties, and in vitro activation by viral and non-viral proteases. The recombinant His-RT exhibited a lower specific activity than the recombinant RT. The latter yielded enzyme activities as high as an Escherichia coli-expressed RT. Removal of the hexahistidine tag from the recombinant His-RT by digestion with enterokinase resulted in a complete loss of enzyme activity. Thus, the hexahistidine tag might be an intrinsic part of the active recombinant His-RT.
Authors:
K Pekrun; H Petry; K D Jentsch; D Moosmayer; G Hunsmann; W Lüke
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  234     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1995 Dec 
Date Detail:
Created Date:  1996-03-11     Completed Date:  1996-03-11     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  811-8     Citation Subset:  IM; X    
Affiliation:
Department for Virology and Immunology, German Primate Centre, Göttingen, Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Baculoviridae / genetics*
Blotting, Western
Cells, Cultured
Chymotrypsin / metabolism
DNA Primers
Gene Expression
Genetic Vectors*
HIV Protease / metabolism
HIV Reverse Transcriptase
HIV-1 / enzymology*
Humans
Insects
Kinetics
Protein Folding
Protein Processing, Post-Translational
RNA-Directed DNA Polymerase / chemistry,  genetics*,  isolation & purification,  metabolism*
Recombinant Proteins / chemistry,  isolation & purification,  metabolism
Trypsin / metabolism
Chemical
Reg. No./Substance:
0/DNA Primers; 0/Recombinant Proteins; EC 2.7.7.49/HIV Reverse Transcriptase; EC 2.7.7.49/RNA-Directed DNA Polymerase; EC 3.4.21.1/Chymotrypsin; EC 3.4.21.4/Trypsin; EC 3.4.23.-/HIV Protease

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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