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Calcium affinity of humanα-actinin 1
Author(s) -
Lars Backman
Publication year - 2015
Publication title -
peerj
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.927
H-Index - 70
ISSN - 2167-8359
DOI - 10.7717/peerj.944
Subject(s) - gene isoform , alternative splicing , isothermal titration calorimetry , actinin , affinities , rna splicing , calcium , biochemistry , calcium binding protein , chemistry , gene , biology , computational biology , rna , organic chemistry , cytoskeleton , cell
Due to alternative splicing, the human ACTN1 gene codes for three different transcripts of α -actinin; one isoform that is expressed only in the brain and two with a more general expression pattern. The sequence difference is located to the C-terminal domains and the EF-hand motifs. Therefore, any functional or structural distinction should involve this part of the protein. To investigate this further, the calcium affinities of these three isoforms of α -actinin 1 have been determined by isothermal calorimetry.

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