• 공업화학
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• 제21권4호
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• pp.424-429
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• 2010

본 연구는 유기발광디바이스용(OLED) 녹색발광재료인 6-알킬-3-크로몬알데히드(2,2-디알킬)하이드라존 유도체의 합성에 관한 것으로서, 유도체들은 탈수축합반응으로 합성되었다. 이들은 전자흡인성의 6-알킬-3-크로몬알데히드류와 전자공여성의 2,2-디알킬하이드라존류의 공액구조를 가지고 있다. 합성된 물질들은 각각 FT-IR, $^1H$-NMR 스펙트럼으로부터 그의 구조적 특성을 확인하였고, 융점, 수득률에 의하여 열적 안정성, 반응성을 확인하였으며, 여기스펙트럼과 발광스펙트럼으로부터 자외가시광과 발광특성을 확인하였다.

• 한국재료학회지
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• 제13권8호
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• pp.514-518
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• 2003

As a fundamental study on organic electroluminescence(EL), blue emitting materials were synthesized and characterized. Individual blue colored hydrazone derivatives were synthesized from the reaction of aldehydes (phthalaldehyde, isophthalaldehyde) with the corresponding amnios (1-methyl -1-phenylhydrazine, 1,1-diphenylhydrazine hydrochloride). Recrystallization of hydrazones from chloroform revealed the melting temperature within $142∼156^{\circ}C$. Photoluminescence(PL) analysis on each hydrazone showed that emission range were blue(458∼478 nm). The structure of obtained hydrazones were elucidated by FT-IR, $^1$H-NMR and C, H, N elemental analyzer.

• 공업화학
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• 제20권6호
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• pp.670-674
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• 2009

본 연구는 유기발광디바이스용(OLED) 녹색형광물질인 3-크로몬알데히드(2,2-이치환)하이드라존 유도체의 합성에 관한 것으로서, 유도체들은 탈수축합반응으로 합성되었다. 이들은 전자흡인성의 3-크로몬알데히드류와 전자공여성의 2,2-이치환하이드라존류의 공액구조를 가지고 있다. 합성한 물질은 각각 FT-IR, $^1H-NMR$ 스펙트럼으로부터 그의 구조적 특성을 확인하였고, 융점, 수득률에 의하여 열적 안정성, 반응성을 확인하였으며, 여기스펙트럼과 발광스펙트럼으로부터 자외가시광과 발광특성을 확인하였다.

• BMB Reports
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• 제32권5호
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• pp.480-485
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• 1999

Tyrosine phenol-lyase of thermophilic Symbiobacterium sp. SC-1, which is obligately and symbiotically dependent on thermophilic Bacillus sp. SK-1, was purified and characterized. The enzyme is composed of four identical subunits and contains approximately 1 mol of pyridoxal 5'-phosphate (PLP) per mol subunit as a cofactor. The enzyme showed absorption maxima at 330 and 420 nm, and lost this absorption profile by treatment with phenylhydrazine. The apparent dissociation constsnt, $K'_D$, for PLP was determined with the apoenzyme to be about $1.2\;{\mu}M$. The isoelectric point was 4.9. The optimal temperature and pH for the $\alpha,\beta$-elimination of L-tyrosine were found to be $80^{\circ}C$ and pH 8.0, respectively. The substrate specificity of the enzyme was very broad: L-amino acids including L-tyrosine, 3,4-dihydroxyphenyl-L-alanine (L-DOPA), L-cysteine, L-serine, S-methyl-L-cysteine, $\beta$-chloro-L-alanine, and S-(o-nitrophenyl)-L-cysteine all served as substrates. D-Tyrosine and D-serine were also decomposed into pyruvic acid and ammonia at rates of 7% and 31% relative to their corresponding L-enantiomers, respectively. D-Alanine, which was inert as a substrate in a, $\beta$-elimination, was the only D-amino acid racemized by the enzyme. The $K_m$ values for L-tyrosine, L-DOPA, S-(o-nitrophenyl)-L-cysteine, $\beta$-chloro-L-alanine, and S-methyl-L-cysteine were 0.19, 9.9, 0.36, 12, and 5.5 mM, respectively.