PARTIAL PURIFICATION AND CHARACTERIZATION OF RESTRICTION ENDONUCLEASE FROM NEISSERIA MENINGITIDIS

Authors
  1. Bhatti, A.R.
  2. Sparling, R.
Corporate Authors
Defence Research Establishment Suffield, Ralston ALTA (CAN);Iowa Univ, Iowa City IA (US) Dept of Microbiology
Abstract
A restriction endonuclease, NmeI, present in Neisseria meningitidis DRES W34 was studied. The enzyme was partially purified by passing through a blue 2 cross-linked agarose column; no contaminating nucleases remained detectable. This enzyme cleaved phage lambda, adenovirus type 2 (Ad 2) and phi x 174 DNA but did not cleave simian virus 40 (SV40) DNA. It had an absolute requirement for Mg super 2 plus for its activity and was inhibited by high concentrations of NaCl or MgCl2. NmeI activity was completely abolished after one hour of incubation at 65C. S-adenosyl-L-methionine and ATP has no effect on its activity suggesting that NmeI is a type II restriction endonuclease enzyme.
Report Number
M-1098 —
Date of publication
15 Dec 1983
Number of Pages
14
DSTKIM No
84-01356
CANDIS No
120793
Format(s):
Hardcopy;Originator's fiche received by DSIS

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