Fluorimetric analysis of recombinant p15 HIV-1 ribonuclease H

We have exploited the sole tryptophan residue (Trp535) in the ribonuclease H (RNase H) domain of human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) to study features of the isolated polypeptide (p15 RNase H) by fluorescence spectroscopy. Incubation of purified p15 RNase H with a sy...

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Veröffentlicht in:	The Journal of biological chemistry 1993-07, Vol.268 (20), p.14743-14749
Hauptverfasser:	CIRINO, N. M, KALAYJIAN, R. C, JENTOFT, J. E, LE GRICE, S. F. J
Format:	Artikel
Sprache:	eng
Schlagworte:	AIDS/HIV Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences DNA - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology HIV Reverse Transcriptase HIV-1 - enzymology human immunodeficiency virus 1 Hydrolases Molecular Sequence Data Peptide Fragments - metabolism Point Mutation Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Ribonuclease H - isolation & purification Ribonuclease H - metabolism RNA - metabolism RNA-Directed DNA Polymerase - chemistry RNA-Directed DNA Polymerase - metabolism Sequence Alignment Spectrometry, Fluorescence Substrate Specificity Tryptophan - chemistry
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