• Journal of the Korean Chemical Society
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• v.51 no.1
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• pp.31-35
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• 2007

The tripodal copper(II) complex [Cu(pmea)(H2O)](ClO4)2·H2O (1) (pmea = bis[(2-pyridyl)methyl]-2-(2-pyridyl)ethylamine) has been synthesized and structurally characterized by X-ray diffraction method. It crystallizes in the triclinic system P-1 with a = 9.9362(9), b = 15.7299(17), c = 18.0562(11) A, α = 68.760(8), β = 76.331(6), γ = 77.092(9)°, V = 2526.2(4) A3, Z = 2. Each copper atom reveals a distorted square pyramidal with three nitrogen atoms of the pmea ligand and water molecule occupying the basal plane and one nitrogen atom from the pyridine ring according the axial position. The cyclic voltammogram of 1 undergoes reversible one-electron oxidation to the CuIII and reversible one-electron reduction to the CuI.

• Food Science of Animal Resources
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• v.34 no.5
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• pp.656-664
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• 2014

The purpose of this study was to analyze myosin heavy chain (MHC) isoforms in bovine longissimus thoracis (LT) muscle by liquid chromatography (LC) and mass spectrometry (MS). LT muscles taken from Hanwoo (Korean native cattle) steer (n=3) used to separate myosin bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The peptide queries were obtained from the myosin bands by LC-MS/MS analysis following in-gel digestion with trypsin. A total of 33 and 43 queries were identified as common and unique peptides, respectively, of MHC isoforms (individual ions scores >43 indicate identity or extensive homology, p<0.05). MHC-1 (IIx), -2 (IIa), -4 (IIb), and -7 (slow/I) were identified based on the Mowse score (5118, 3951, 2526, and 2541 for MHC-1, -2, -4, and -7, respectively). However, more analysis is needed to confirm the expression of MHC-4 in bovine LT muscle because any query identified as a unique peptide of MHC-4 was not found. The queries that were identified as unique peptides could be used as peptide markers to confirm MHC-1 (14 queries), -2 (8 queries), and -7 (21 queries) in bovine LT muscle; no query identified as a unique peptide of MHC-4 was found. LC-MS/MS analysis is a useful approach to study MHC isoforms at the protein level.