78
suggests that copsin serves as the basis for the synthesis of new antibiotics (Essig
et al. 2014).
A ribonuclease (RNase) was isolated from fresh fruiting bodies of the mushroom
Pleurotus sajor-caju. Its optimal pH and molecular mass were 5.5 and 12 kDa,
respectively. It had preferential activity for poly (U) and with much lower activity
toward poly (A), poly (G), and poly (C). The ribonuclease exhibited some activity
toward herring sperm DNA and calf thymus DNA. Ribonuclease activity was not
affected in the presence of KCl (10 and 100 mM) and NaCl (100 mM and 1 M), but
was strongly inhibited by CuSO 4 (0.01 and 0.1 mM). Divalent salts such as MgCl 2 ,
CaCl 2 , ZnCl 2 , ZnSO 4 , and FeSO 4 inhibited with less power than CuSO 4 . The ribonuclease was stable up to 60 °C for 1 h. The ribonuclease inhibited growth of bacteria Pseudomonas aeruginosa and Staphylococcus aureus and of the mycelial of
the fungi Fusarium oxysporum and Mycosphaerella arachidicola. Ribonuclease
decreased the viability of the tumor cells HepG2 (hepatoma) and L1210 (leukemia)
which was reduced with an IC 50 of 0.22 and 0.1 μM, respectively, and also inhibited
translation in a cell-free rabbit reticulocyte lysate system (IC 50 of 158 nM) and
methyl-thymidine uptake by murine splenocytes (IC 50 of 65 nM) (Ngai and
Ng 2004).
An RNase (14.6 kDa) was isolated from dried fruiting bodies of the edible mushroom Lactarius flavidulus. Its optimum pH and temperature were 5.5 and 70 °C,
respectively. The ranking of its activity toward various polyhomoribonucleotides
was poly (C) > poly (G) > poly (A) > poly (U). It inhibited proliferation of HepG2
cells and L1210 cells with an IC 50 of 3.19 μM and 6.52 μM, respectively. It also
suppressed the activity of HIV-1 reverse transcriptase with an IC 50 of 2.55 μM (Wu
et al. 2012).
A novel 15 kDa RNase was purified from Pleurotus djamor. Its N-terminal
amino acid sequence was different from those previously reported RNase sequences
of mushrooms belonging to the genus of Pleurotus and other genera. It exhibited
maximal RNase activity at pH 4.6 and 60 °C. Its activity toward polyhomoribonucleotides was poly (U) > poly (C) > poly (A) > poly (G). RNase inhibited proliferation of hepatoma cells and breast cancer cells. The ranking of inhibitory potencies
of metal ions on RNase activity was Fe (3
+
) > Al (3
+
) > Ca (2
+
) > Hg (2
+
) (Wu
et al. 2010).
An RNase was purified from dried fruiting bodies of the wild mushroom Amanita
hemibapha. Its molecular mass was 45 kDa and exhibited maximal RNase activity
at pH 5 and in a temperature range between 60 and 70 °C. It did not show ribonucleolytic activity toward four polyhomoribonucleotides. The amino acid sequence
(GDDETFWEHEWAK) showed this RNase was a ribonuclease T2-like RNase. It
had strong inhibitory activity against HIV-1 reverse transcriptase (HIV-1 RT) with
an IC 50 of 17 μM (Sekete et al. 2012).
A novel RNase with molecular mass of 18 kDa was purified from fresh fruiting
bodies of Hypsizygus marmoreus. Its maximal RNase activity was at pH 5 and
70 °C. RNase showed the highest ribonucleolytic activity toward poly (C) (196 U/
mg), followed by poly (A) (126 U/mg), and less activity toward poly (U) (48 U/mg)
G. Díaz-Godínez and R. Díaz
suggests that copsin serves as the basis for the synthesis of new antibiotics (Essig
et al. 2014).
A ribonuclease (RNase) was isolated from fresh fruiting bodies of the mushroom
Pleurotus sajor-caju. Its optimal pH and molecular mass were 5.5 and 12 kDa,
respectively. It had preferential activity for poly (U) and with much lower activity
toward poly (A), poly (G), and poly (C). The ribonuclease exhibited some activity
toward herring sperm DNA and calf thymus DNA. Ribonuclease activity was not
affected in the presence of KCl (10 and 100 mM) and NaCl (100 mM and 1 M), but
was strongly inhibited by CuSO 4 (0.01 and 0.1 mM). Divalent salts such as MgCl 2 ,
CaCl 2 , ZnCl 2 , ZnSO 4 , and FeSO 4 inhibited with less power than CuSO 4 . The ribonuclease was stable up to 60 °C for 1 h. The ribonuclease inhibited growth of bacteria Pseudomonas aeruginosa and Staphylococcus aureus and of the mycelial of
the fungi Fusarium oxysporum and Mycosphaerella arachidicola. Ribonuclease
decreased the viability of the tumor cells HepG2 (hepatoma) and L1210 (leukemia)
which was reduced with an IC 50 of 0.22 and 0.1 μM, respectively, and also inhibited
translation in a cell-free rabbit reticulocyte lysate system (IC 50 of 158 nM) and
methyl-thymidine uptake by murine splenocytes (IC 50 of 65 nM) (Ngai and
Ng 2004).
An RNase (14.6 kDa) was isolated from dried fruiting bodies of the edible mushroom Lactarius flavidulus. Its optimum pH and temperature were 5.5 and 70 °C,
respectively. The ranking of its activity toward various polyhomoribonucleotides
was poly (C) > poly (G) > poly (A) > poly (U). It inhibited proliferation of HepG2
cells and L1210 cells with an IC 50 of 3.19 μM and 6.52 μM, respectively. It also
suppressed the activity of HIV-1 reverse transcriptase with an IC 50 of 2.55 μM (Wu
et al. 2012).
A novel 15 kDa RNase was purified from Pleurotus djamor. Its N-terminal
amino acid sequence was different from those previously reported RNase sequences
of mushrooms belonging to the genus of Pleurotus and other genera. It exhibited
maximal RNase activity at pH 4.6 and 60 °C. Its activity toward polyhomoribonucleotides was poly (U) > poly (C) > poly (A) > poly (G). RNase inhibited proliferation of hepatoma cells and breast cancer cells. The ranking of inhibitory potencies
of metal ions on RNase activity was Fe (3
+
) > Al (3
+
) > Ca (2
+
) > Hg (2
+
) (Wu
et al. 2010).
An RNase was purified from dried fruiting bodies of the wild mushroom Amanita
hemibapha. Its molecular mass was 45 kDa and exhibited maximal RNase activity
at pH 5 and in a temperature range between 60 and 70 °C. It did not show ribonucleolytic activity toward four polyhomoribonucleotides. The amino acid sequence
(GDDETFWEHEWAK) showed this RNase was a ribonuclease T2-like RNase. It
had strong inhibitory activity against HIV-1 reverse transcriptase (HIV-1 RT) with
an IC 50 of 17 μM (Sekete et al. 2012).
A novel RNase with molecular mass of 18 kDa was purified from fresh fruiting
bodies of Hypsizygus marmoreus. Its maximal RNase activity was at pH 5 and
70 °C. RNase showed the highest ribonucleolytic activity toward poly (C) (196 U/
mg), followed by poly (A) (126 U/mg), and less activity toward poly (U) (48 U/mg)
G. Díaz-Godínez and R. Díaz