HIV-1 reverse transcriptase purified from a recombinant strain of Escherichia coli.
A better understanding of the structure and biochemical properties of the replicative machinery of human immunodeficiency virus type 1 (HIV-1) may be useful in the screening and design of drugs that could be used to treat AIDS. We have previously described a recombinant strain of Escherichia coli that produces HIV-1 reverse transcriptase (RT). Fermentation conditions for the large-scale growth of the bacterial strain and a protocol for the purification of an enzymatically active 66-Kd form of the RT have been developed. The purified RT has all of the appropriate enzymatic functions and properties. The recombinant protein can be substituted for the viral enzyme in structural and biochemical studies and used in screens for drugs that could inhibit HIV replication.
Program Resources, Inc., NCI-Frederick Cancer Research and Development Center, Maryland 21701-1013.
P K
PK
Clark
A L
AL
Ferris
D A
DA
Miller
A
A
Hizi
K W
KW
Kim
S M
SM
Deringer-Boyer
M L
ML
Mellini
A D
AD
Clark
G F
GF
Arnold
W B
WB
Lebherz
D001709:Biotechnology; D004259:DNA-Directed DNA Polymerase / Q000302:isolation & purification; D004355:Drug Stability; D004722:Endoribonucleases / Q000302:isolation & purification; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005285:Fermentation; D015497:HIV-1 / Q000201:enzymology* / Q000235:genetics; D012194:RNA-Directed DNA Polymerase / Q000235:genetics / Q000302:isolation & purification*; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification; D016914:Ribonuclease H; D013379:Substrate Specificity
D011994:Recombinant Proteins; D012194:RNA-Directed DNA Polymerase; D004259:DNA-Directed DNA Polymerase; D004722:Endoribonucleases; D016914:Ribonuclease H