scholarly journals Processivity Clamp gp45 and ssDNA-Binding-Protein gp32 Modulate the Fidelity of Bacteriophage RB69 DNA Polymerase in a Sequence-Specific Manner, Sometimes Enhancing and Sometimes Compromising Accuracy

Genetics ◽  
2005 ◽  
Vol 169 (4) ◽  
pp. 1815-1824 ◽  
Author(s):  
Anna Bebenek ◽  
Geraldine T. Carver ◽  
Farid A. Kadyrov ◽  
Grace E. Kissling ◽  
John W. Drake
1995 ◽  
Vol 23 (13) ◽  
pp. 2389-2395 ◽  
Author(s):  
Marten P. Smidt ◽  
Bernadetta Russchen ◽  
Lenie Snippe ◽  
Jan Wilnholds ◽  
Geert AB

Structure ◽  
2018 ◽  
Vol 26 (5) ◽  
pp. 722-733.e2 ◽  
Author(s):  
Neil R. Lloyd ◽  
Deborah S. Wuttke

1998 ◽  
Vol 79 (5) ◽  
pp. 1257-1264 ◽  
Author(s):  
T Tsurumi ◽  
N Yokoyama ◽  
Y Yamashita ◽  
J Kishore ◽  
H Yamada ◽  
...  

1986 ◽  
Vol 233 (3) ◽  
pp. 913-916 ◽  
Author(s):  
F S Sharief ◽  
S H Wilson ◽  
S S-L Li

A 36,000-Mr protein purified from mouse myeloma on the basis of selective binding to a single-stranded DNA (ssDNA)-cellulose column has been identified as the lactate dehydrogenase A (LDH-A) subunit. A homogeneous preparation of this mouse myeloma ssDNA-binding protein, termed the ‘low-salt-eluting protein’, was found to possess LDH activity, and rabbit antiserum prepared against this protein was shown to cross-react with purified 36,000-Mr LDH-A subunits from mouse and bovine sources. In addition, bovine and human LHD-A4 isoenzymes were shown to be capable of binding ssDNA. These enzymic and immunological identities with LDH-A were not observed with purified helix-destabilizing protein 1 from mouse myeloma. A model for ssDNA-LDH binding is discussed.


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