• 대한화학회지
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• 제51권1호
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• pp.31-35
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• 2007

트리포달 구리(II) 착물 [Cu(pmea)(H2O)](ClO4)2·H2O (1) (pmea=bis[(2-pyridyl)methyl]-2-(2-pyridyl)-ethylamine)을 합성하고 X-선 회절법으로 구조를 규명하였다. 이 착물은 삼사정계, 공간군 P-1, a = 9.9362(9) A, b = 15.7299(17) A, c = 18.0562(11) A, α = 68.760(8)°, β = 76.331(6)°, γ = 77.092(9)°, V = 2526.2(4) A3, Z = 2로 결정화 되었다. 각각의 구리 원자는 약간 일그러진 사각뿔 구조를 갖는데, 바탕 면은 pmea 리간드에 있는 세 개의 질소원자와 물 분자가 포함되어 있으며 축 방향에는 피리딘 고리의 질소 원자가 포함되어있다. 착물 1의 순환 전압전류 그림은 가역 일-전자 산화 CuIII 및 환원 CuI 과정으로 진행됨을 보여주었다.

• 한국축산식품학회지
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• 제34권5호
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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.