摘要
报道了牛血清白蛋白（ＢＳＡ）、血红蛋白（Ｈｂ）和γ－球蛋白（γ－Ｇｂ）同银（Ⅰ）－铜（Ⅱ）离子配合物的ＩＲ、Ｒａｍａｎ和ＵＶ／ＶＩＳ光谱的详情。在所研究的配合物中，蛋白质分子起着阴离子配位基的作用。在ｐＨ１０．５的Ｂ４Ｏ７２－－ＯＨ－缓冲介质中，蛋白质－银－铜配合物表现出强烈的橙黄色，最大吸收位于２８５和４１０～４１５ｎｍ区域。固态配合物的ＦＴ－ＩＲ光谱和它们对应的蛋白质比较，在１７００～１１００ｃｍ－１范围呈现强烈差异。Ｒａｍａｎ光谱的特征带位于１６００～１１００ｃｍ－１区域。这些结果表明，Ａｇ（Ⅰ）－Ｃｕ（Ⅱ）离子同蛋白质中羧基的氧和胺基或酰胺基的氮形成强烈配位的混配配合物。
The preparation, IR, surface enhanced Raman scattering (SERS) and UV/VIS
spectroscopic properties of some proteins bavine serum albumin (BSA), hemoglobin (Hb) and
γ globuin (γ Gb) with silver (Ⅰ) copper (Ⅱ) ion complexes are reported. It is suggested that
the protein molecules act as chelate anionic ligand in all the complexes studied. The protein Ag
Cu complexes appear strong orange yellow colour when SDS and formaldehyde are present in
pH10.5 B 4O 7 2- OH - buffer, with maxium absorption near 285 and 410￣415nm region.
The FT IR spectra showed obvious difference in 1700￣1100 cm -1 region for all the
proteins studied compared with their Ag (Ⅰ) Cu(Ⅱ) complexes. The characteristic bands of
SERS appeared in 1620￣1100 cm -1 region. The results show that Ag Cu ions form strong
binding coordination compounds with proteins via oxygen of carboxylate and nitrogen of amine
or amide groups.
出处
《化学试剂》
CAS
CSCD
1999年第1期11-14,共4页
Chemical Reagents
基金
贵州省科学基金
关键词
蛋白质
银
铜
配合物
混配配合物
proteins, silver copper ion complexes, FT IR, Raman, UV/VIS
spectra
