Open AccessCharacterization of the pH 4.0 Endonuclease from Adenovirus‐Type‐2‐Infected KB Cells
Author(s) -
REIF Ulrike,
WINTERHOFF Ute,
DOERFLER Walter
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11322.x
Subject(s) - endonuclease , cleavage (geology) , enzyme , restriction enzyme , dna , microbiology and biotechnology , chemistry , adenoviridae , biology , biochemistry , recombinant dna , gene , paleontology , fracture (geology)
The properties of the pH 4.0 endonuclease from adenovirus‐type‐2‐infected KB cells were determined. The enzyme has a molecular weight of approximately 40 000. Its pH optimum is at pH 4.0, it is not inhibited by ethylenediaminetetraacetate (EDTA), and it is active at temperatures up to 60 °C. The enzyme cleaves adenovirus DNA in a stepwise manner. The limit digestion product has a molecular weight of 120 000–200 000. There is evidence that the cleavage reaction proceeds via an initial single‐strand nick. Under the conditions tested the endonuclease did not seem to reveal a high degree of specificity as to the recognition of cleavage sites, or else the sites recognized occurred very frequently.