Purification and characterization of the 2nd 5'-nucleotide-forming nuclease from Lentinus edodes.
The 2nd endonuclease (nuclease Le3) which hydrolyzes both RNA and heat denatured DNA to 5'-nucleotides was purified from the fruit bodies of Lentinus edodes to a homogeneous state by SDS PAGE. The nuclease was different from the nuclease Le1 previously characterized [H. Shimada et al. Chem. Pharm. Bull., 39, 2633-2637 (1991)] in molecular weight, optimal pH and N-terminal amino acid sequence. The N-terminal amino acid sequence of nuclease Le3 analyzed up to the 20th residue showed that 50% of the amino acid residues are identical to nuclease Le1.
Kobayashi
H
H
Department of Microbiology, College of Pharmacy, Nihon University, Chiba.
Inokuchi
N
N
Koyama
T
T
Tomita
M
M
Irie
M
M
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004706:Endodeoxyribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004722:Endoribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011124:Polyporaceae / Q000201:enzymology*
D004706:Endodeoxyribonucleases; D004722:Endoribonucleases; C094691:endonuclease Le(3)