Extracellular ATP binding proteins as potential receptors in mucociliary epithelium: Characterization using [32P]3?-O-(4-benzoyl)benzoyl ATP, a photoaffinity label

1995 ◽  
Vol 147 (1) ◽  
Author(s):  
L. Gheber ◽  
Z. Priel ◽  
C. Aflalo ◽  
V. Shoshan-Barmatz
Keyword(s):  
Binding Proteins ◽  
Extracellular Atp ◽  
Atp Binding ◽  
Photoaffinity Label

3′-Arylazido-8-azido ATP—A cross-linking photoaffinity label for ATP binding proteins

1980 ◽  
Vol 95 (2) ◽  
pp. 562-568 ◽  
Author(s):  
Hans-Jochen Schäfer ◽  
Peter Scheurich ◽  
Gabriele Rathgeber ◽  
Klaus Dose ◽  
Annelore Mayer ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Cross Linking ◽  
Atp Binding ◽  
Photoaffinity Label

scholarly journals Isotope-Coded ATP Probe for Quantitative Affinity Profiling of ATP-Binding Proteins

2013 ◽  
Vol 85 (15) ◽  
pp. 7478-7486 ◽  
Author(s):  
Yongsheng Xiao ◽  
Lei Guo ◽  
Yinsheng Wang
Keyword(s):  
Binding Proteins ◽  
Atp Binding

scholarly journals Affinity labeling of annexin VI with a triazine dye, Cibacron blue 3GA. Probable interaction of the dye with C-terminal nucleotide-binding site within the annexin molecule.

1999 ◽  
Vol 46 (2) ◽  
pp. 419-429 ◽  
Author(s):  
M Danieluk ◽  
R Buś ◽  
S Pikuła ◽  
J Bandorowicz-Pikuła
Keyword(s):  
Binding Site ◽  
Binding Proteins ◽  
Direct Sequencing ◽  
Nucleotide Binding ◽  
Atp Binding ◽  
Dependent Manner ◽  
Cibacron Blue ◽  
Annexin Vi ◽  
Cibacron Blue 3Ga ◽  
Triazine Dye

Annexin VI (AnxVI) from porcine liver, a member of the annexin family of Ca(2+)- and membrane-binding proteins, has been shown to bind ATP in vitro with a K(d) in the low micromolar concentration range. However, this protein does not contain within its primary structure any ATP-binding consensus motifs found in other nucleotide-binding proteins. In addition, binding of ATP to AnxVI resulted in modulation of AnxVI function, which was accompanied by changes in AnxVI affinity to Ca2+ in the presence of ATP. Using limited proteolytic digestion, purification of protein fragments by affinity chromatography on ATP-agarose, and direct sequencing, the ATP-binding site of AnxVI was located in a C-terminal half of the AnxVI molecule. To further study AnxVI-nucleotide interaction we have employed a functional nucleotide analog, Cibacron blue 3GA (CB3GA), a triazine dye which is commonly used to purify multiple ATP-binding proteins and has been described to modulate their activities. We have observed that AnxVI binds to CB3GA immobilized on agarose in a Ca(2+)-dependent manner. Binding is reversed by EGTA and by ATP and, to a lower extent, by other adenine nucleotides. CB3GA binds to AnxVI also in solution, evoking reversible aggregation of protein molecules, which resembles self-association of AnxVI molecules either in solution or on a membrane surface. Our observations support earlier findings that AnxVI is an ATP-binding protein.

scholarly journals The ABCF gene family facilitates disaggregation during animal development

2020 ◽  
Vol 31 (13) ◽  
pp. 1324-1345
Author(s):  
Sydney Skuodas ◽  
Amy Clemons ◽  
Michael Hayes ◽  
Ashley Goll ◽  
Betul Zora ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Gene Family ◽  
Early Development ◽  
Binding Proteins ◽  
Atp Binding ◽  
Animal Development ◽  
Developmental Program ◽  
Animal Genomes

Skuodas and Clemons et al. show that protein aggregation is pervasive during early development and that the ABCF family of soluble ATP-binding proteins, which are encoded by animal genomes and expressed embryonically, regulate disaggregation and are instrumental for a normal developmental program.

Sign in / Sign up

Export Citation Format

Share Document