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Troponin T from the Japanese Pearl Oyster Pinctada fucata: Molecular Cloning, Tissue Distribution, Gene Structure, and Interaction Analysis with …

 Biomedical & Life Sciences. 2020; 
comment Daisuke Funabaraorcid, Yoshinori Urakawa, Daisuke Ishikawa, Satoshi Kanoh
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Codon Optimization Pifuc-TnT was prepared as previously reported with some modifications [13]. Briefly, Pifuc-TnT was expressed in Escherichia coli as a histidine-tagged protein. A DNA fragment codon-optimized for expression in E. coli and encoding the full length of the open reading frames was commercially synthesized (GenScript, Piscataway, NJ, USA). The plasmid pET15b (Novagen, Darmstadt, Germany) was used to create the expression vector pET-Pifuc-TnT. E. coli BL21 (DE3) cells were transformed with pET-Pifuc-TnT and cultured in auto-induction media at 37˚C for 24 h [28]. Get A Quote

摘要

Troponin (Tn) is composed of three subunits (TnI, TnC and TnT) that bind Ca2+ and regulate striated muscle contraction in vertebrates. TnT’s function has been extensively described in vertebrates, but its role has been obscure in molluscan muscles. Our previous work indicated that the TnC and TnI subunits work in adductor phasic muscle, but not in catch muscle. Here, we have characterized TnT from the Japanese bivalve pearl oyster Pinctada fucata to start to explain the function of Tn in molluscan muscle contraction. We determined the primary structure of the full-length TnT protein from the P. fucataadductor muscle (Pifuc-TnT), and found that it is composed of 316 amino acid residues with a predicted mol... More

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