TY - JOUR
T1 - Partial purification and properties of an endoribonuclease isolated from human KB cells
AU - Bothwell, A. L.M.
AU - Altman, S.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1975
Y1 - 1975
N2 - With the use of a precursor to Escherichia coli tRNA(Tyr) as substrate, the authors have detected and partially purified a novel endoribonuclease from the cytoplasm of human KB tissue culture cells. This activity, which has been called RNase NU, cleaves the tRNA precursor at two sites in that part of the molecule which is not included in the mature tRNA sequence and which is normally degraded in vivo. In keeping with this observation, it has been found that, of a variety of substrates tested, only those which are unstable in vivo are attacked by RNase NU. RNase NU can be purified from the 0.2 M NH4Cl wash of ribosomes followed by ammonium sulfate fractionation and DEAE Sephadex chromatography. RNase NU cleaves RNA to create 3' phosphate terminated oligonucleotides. It has a pH optimum near 8.0, requires either a monovalent cation (NH4+ is most efficient) or Ca for optimal activity, and is inhibited by 0.1 M phosphate. In the course of purifying RNase NU, the authors detected and studied the intracellular distribution of other ribonuclease activities in human KB cells.
AB - With the use of a precursor to Escherichia coli tRNA(Tyr) as substrate, the authors have detected and partially purified a novel endoribonuclease from the cytoplasm of human KB tissue culture cells. This activity, which has been called RNase NU, cleaves the tRNA precursor at two sites in that part of the molecule which is not included in the mature tRNA sequence and which is normally degraded in vivo. In keeping with this observation, it has been found that, of a variety of substrates tested, only those which are unstable in vivo are attacked by RNase NU. RNase NU can be purified from the 0.2 M NH4Cl wash of ribosomes followed by ammonium sulfate fractionation and DEAE Sephadex chromatography. RNase NU cleaves RNA to create 3' phosphate terminated oligonucleotides. It has a pH optimum near 8.0, requires either a monovalent cation (NH4+ is most efficient) or Ca for optimal activity, and is inhibited by 0.1 M phosphate. In the course of purifying RNase NU, the authors detected and studied the intracellular distribution of other ribonuclease activities in human KB cells.
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M3 - Article
C2 - 1089659
AN - SCOPUS:0016608288
SN - 0021-9258
VL - 250
SP - 1451
EP - 1459
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 4
ER -