Structure-function analysis of DNA polymerase-.beta. using monoclonal antibodies: identification of a putative nucleotide binding domain

Biochemistry ◽  
1992 ◽  
Vol 31 (34) ◽  
pp. 7989-7997 ◽  
Author(s):  
Anthony J. Recupero ◽  
Diane C. Rein ◽  
Ralph R. Meyer
Biochemistry ◽  
1995 ◽  
Vol 34 (49) ◽  
pp. 15934-15942 ◽  
Author(s):  
Karen L. Menge ◽  
Zdenek Hostomsky ◽  
Beverly R. Nodes ◽  
Geoffrey O. Hudson ◽  
Soheil Rahmati ◽  
...  

1990 ◽  
Vol 265 (4) ◽  
pp. 2124-2131
Author(s):  
A Kumar ◽  
S G Widen ◽  
K R Williams ◽  
P Kedar ◽  
R L Karpel ◽  
...  

1991 ◽  
Vol 279 (1) ◽  
pp. 203-212 ◽  
Author(s):  
R E A Tunwell ◽  
J W Conlan ◽  
I Matthews ◽  
J M East ◽  
A G Lee

Epitopes for monoclonal antibodies binding to the native (Ca(2+)-Mg2+)-ATPase have been defined by studying binding to sets of hexameric peptides synthesized on plastic pegs. Epitopes have been confirmed by demonstrating the binding of anti-peptide antibodies to the ATPase. A method is presented for definition of surface-exposed epitopes using polyclonal antibodies. Three surface-exposed epitopes have been defined in the nucleotide-binding domain of the ATPase, suggesting considerable surface exposure of this region. Other surface-exposed epitopes have been located in the region of the fourth stalk domain.


Biochemistry ◽  
2008 ◽  
Vol 47 (31) ◽  
pp. 8048-8057 ◽  
Author(s):  
Drew L. Murphy ◽  
Jessica Kosa ◽  
Joachim Jaeger ◽  
Joann B. Sweasy

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