001     56497
005     20200402205905.0
024 7 _ |2 pmid
|a pmid:17218469
024 7 _ |2 pmc
|a pmc:PMC1852358
024 7 _ |2 DOI
|a 10.1529/biophysj.106.094847
024 7 _ |2 WOS
|a WOS:000245544100028
037 _ _ |a PreJuSER-56497
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biophysics
100 1 _ |a Haber-Pohlmeier, S.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB12272
245 _ _ |a Binding of Ca2+ to glutamic acid-rich polypeptides from the rod outer segment
260 _ _ |a New York, NY
|b Rockefeller Univ. Press
|c 2007
300 _ _ |a 3207 - 3214
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Biophysical Journal
|x 0006-3495
|0 882
|v 92
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Rod photoreceptors contain three different glutamic acid-rich proteins (GARPs) that have been proposed to control the propagation of Ca(2+) from the site of its entry at the cyclic nucleotide-gated channel to the cytosol of the outer segment. We tested this hypothesis by measuring the binding of Ca(2+) to the following five constructs related to GARPs of rod photoreceptors: a 32-mer peptide containing 22 carboxylate groups, polyglutamic acid, a recombinant segment comprising 73 carboxylate groups (GLU), GARP1, and GARP2. Ca(2+) binding was investigated by means of a Ca(2+)-sensitive electrode. In all cases, Ca(2+) binds with low affinity; the half-maximum binding constant K(1/2) ranges from 6 to 16 mM. The binding stoichiometry between Ca(2+) ions and carboxylic groups is approximately 1:1; an exception is GARP2, where a binding stoichiometry of approximately 1:2 was found. Hydrodynamic radii of 1.6, 2.8, 3.3, 5.7, and 6.7 nm were determined by dynamic light scattering for the 32-mer, polyglutamic acid, GLU, GARP2, and GARP1 constructs, respectively. These results suggest that the peptides as well as GARP1 and GARP2 do not adopt compact globular structures. We conclude that the structures should be regarded as loose coils with low-affinity, high-capacity Ca(2+) binding.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Calcium: chemistry
650 _ 2 |2 MeSH
|a Glutamic Acid: chemistry
650 _ 2 |2 MeSH
|a Nerve Tissue Proteins: chemistry
650 _ 2 |2 MeSH
|a Peptides: chemistry
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Retinal Rod Photoreceptor Cells: chemistry
650 _ 7 |0 0
|2 NLM Chemicals
|a Nerve Tissue Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptides
650 _ 7 |0 56-86-0
|2 NLM Chemicals
|a Glutamic Acid
650 _ 7 |0 7440-70-2
|2 NLM Chemicals
|a Calcium
650 _ 7 |a J
|2 WoSType
700 1 _ |a Abarca Heidemann, K.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB15797
700 1 _ |a Körschen, H. G.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB31218
700 1 _ |a Kaur Dhiman, H.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Heberle, J.
|b 4
|u FZJ
|0 P:(DE-Juel1)VDB572
700 1 _ |a Schwalbe, H.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Klein-Seetharaman, J.
|b 6
|u FZJ
|0 P:(DE-Juel1)VDB44599
700 1 _ |a Kaupp, U. B.
|b 7
|u FZJ
|0 P:(DE-Juel1)VDB728
700 1 _ |a Pohlmeier, A.
|b 8
|u FZJ
|0 P:(DE-Juel1)VDB1270
773 _ _ |a 10.1529/biophysj.106.094847
|g Vol. 92, p. 3207 - 3214
|p 3207 - 3214
|q 92<3207 - 3214
|0 PERI:(DE-600)1477214-0
|t Biophysical journal
|v 92
|y 2007
|x 0006-3495
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1852358
909 C O |o oai:juser.fz-juelich.de:56497
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|b Gesundheit
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914 1 _ |y 2007
915 _ _ |0 StatID:(DE-HGF)0010
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|d 31.10.2010
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|l Zelluläre Biophysik
|d 31.12.2008
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920 1 _ |k INB-2
|l Molekulare Biophysik
|d 31.12.2008
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