TY - JOUR
T1 - A neutral DNase in venom sac extract of the oriental hornet Vespa orient alis
T2 - Characterization, specificity and mode of action
AU - Ring, B.
AU - Ishay, J.
AU - Slor, H.
N1 - Funding Information:
Acknowledgement-This research was supported in part by a grant from the Israel Cancer Association (to H .S .1~
PY - 1981
Y1 - 1981
N2 - A neutral DNase was purified by acrylamide gel electrophoresis from venom sac extracts of the Oriental hornet (Vespa orientalis). The DNase is active optimally at pH 7 in 0·05 M Tris-HCl buffer. Addition of NaCl inhibited the DNase activity, and with 0·15 M NaCl the enzyme was completely inhibited. RNA addition also inhibited the enzyme activity. Divalent cations were essential for enzymatic activity. At 1 mM concentrations, MgCl2 was the best activator while MnCl2 and CaCl2 activations were, respectively, about 75% and 25% that of the magnesium salt. EDTA completely inhibited DNase activity. The DNase was characterized as an endonuclease by its ability to nick circular supercoiled PM2 DNA. It is equally active on both native and single-stranded DNA as substrates and produces oligonucleotides terminated by 5′ phosphate and 3′ hydroxyl groups. The enzyme is free of RNase and of non-specific phosphodiesterase activities.
AB - A neutral DNase was purified by acrylamide gel electrophoresis from venom sac extracts of the Oriental hornet (Vespa orientalis). The DNase is active optimally at pH 7 in 0·05 M Tris-HCl buffer. Addition of NaCl inhibited the DNase activity, and with 0·15 M NaCl the enzyme was completely inhibited. RNA addition also inhibited the enzyme activity. Divalent cations were essential for enzymatic activity. At 1 mM concentrations, MgCl2 was the best activator while MnCl2 and CaCl2 activations were, respectively, about 75% and 25% that of the magnesium salt. EDTA completely inhibited DNase activity. The DNase was characterized as an endonuclease by its ability to nick circular supercoiled PM2 DNA. It is equally active on both native and single-stranded DNA as substrates and produces oligonucleotides terminated by 5′ phosphate and 3′ hydroxyl groups. The enzyme is free of RNase and of non-specific phosphodiesterase activities.
UR - https://www.scopus.com/pages/publications/0019414947
U2 - 10.1016/0041-0101(81)90027-1
DO - 10.1016/0041-0101(81)90027-1
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C2 - 6267738
AN - SCOPUS:0019414947
SN - 0041-0101
VL - 19
SP - 241
EP - 247
JO - Toxicon
JF - Toxicon
IS - 2
ER -