Photoaffinity Labeling of Creatine Kinase with 2-Azido- and 8-Azidoadenosine Triphosphate: Identification of Two Peptides from the ATP-Binding Domain

Biochemistry ◽  
1994 ◽  
Vol 33 (39) ◽  
pp. 11935-11941 ◽  
Author(s):  
Michael C. Olcott ◽  
Mary L. Bradley ◽  
Boyd E. Haley
Keyword(s):  
Creatine Kinase ◽  
Photoaffinity Labeling ◽  
Binding Domain ◽  
Atp Binding

Photoaffinity labeling of the ATP binding domain of Rubisco activase and a separate domain involved in the activation of ribulose-1,5-bisphosphate carboxylase/oxygenase

Biochemistry ◽  
1994 ◽  
Vol 33 (49) ◽  
pp. 14879-14886 ◽  
Author(s):  
Michael E. Salvucci ◽  
Ashok J. Chavan ◽  
Robert R. Klein ◽  
Krishnan Rajagopolan ◽  
Boyd E. Haley
Keyword(s):  
Photoaffinity Labeling ◽  
Rubisco Activase ◽  
Binding Domain ◽  
Atp Binding ◽  
Bisphosphate Carboxylase

Identification of the creatine binding domain of creatine kinase by photoaffinity labeling

1998 ◽  
Vol 1387 (1-2) ◽  
pp. 80-88 ◽  
Author(s):  
Kyung-Lyum Min ◽  
Jean-Paul Steghens ◽  
Robert Henry ◽  
Alain Doutheau ◽  
Christian Collombel
Keyword(s):  
Creatine Kinase ◽  
Photoaffinity Labeling ◽  
Binding Domain

Phosphate Binding to Isolated Chloroplast Coupling Factor (CF1)

1988 ◽  
Vol 43 (3-4) ◽  
pp. 213-218 ◽  
Author(s):  
Bernhard Huchzermeyer
Keyword(s):  
Atpase Activity ◽  
Binding Site ◽  
Inorganic Phosphate ◽  
Coupling Factor ◽  
Binding Domain ◽  
Atp Binding ◽  
Phosphate Binding ◽  
Chloroplast Coupling Factor ◽  
Single Binding Site ◽  
Site Binding

A single binding site for phosphate was found on isolated chloroplast coupling factor in the absence of nucleotides. In our experiments the phosphate binding site showed a Kd of 170 μᴍ. We did not observe any differences whether the ATPase activity of CF] had been activated or not. If the enzyme was incubated with [γ-32P]ATP the amount of 32P bound per CF1 depended on the pretreatment of the enzyme: In the presence of ADP no ATP or phosphate was bound to CF,. After activation of ATPase activity one mol of ATP per mol CF, was rapidly bound and hydrolyzed while there was a slowly occurring binding of another phosphate without concomitant nucleotide binding. We conclude that there are two different types of phosphate binding observed in our experiments: 1) Inorganic phosphate can be bound by one catalytic site per mol of CF1 2) The γ-phosphate of ATP is able to bind to an ATP binding domain of the enzyme if this domain can exchange substrates with the incubation medium. This ATP binding domain appears to differ from the site binding inorganic phosphate, because at least a portion of the coupling factor contains more than one labelled phosphate during our ATPase tests.

scholarly journals Dissection of the ATP-binding Domain of the Chaperone hsc70 for Interaction with the Cofactor Hap46

2000 ◽  
Vol 276 (13) ◽  
pp. 10178-10184 ◽  
Author(s):  
Gabriele Petersen ◽  
Christian Hahn ◽  
Ulrich Gehring
Keyword(s):  
Binding Domain ◽  
Atp Binding

Localization by Photoaffinity Labeling of Natriuretic Peptide Receptor-A Binding Domain†

Biochemistry ◽  
1996 ◽  
Vol 35 (39) ◽  
pp. 12950-12956 ◽  
Author(s):  
Normand McNicoll ◽  
Jean Gagnon ◽  
Jean-Jacques Rondeau ◽  
Huy Ong ◽  
André De Léan
Keyword(s):  
Natriuretic Peptide ◽  
Photoaffinity Labeling ◽  
Binding Domain ◽  
Natriuretic Peptide Receptor ◽  
Peptide Receptor ◽  
Natriuretic Peptide Receptor A
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