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Metabolic Changes in Rats with Photochemically Induced Cerebral Infarction and the Effects of Batroxobin:A Study by Magnetic Resonance Imaging,~1H-and ^(31)p-Magnetic Resonance Spectroscopy 被引量:6
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作者 管兴志 吴卫平 +6 位作者 匡培根 匡培梓 高杨 管林初 李丽云 毛希安 刘买利 《Journal of Traditional Chinese Medicine》 SCIE CAS CSCD 2001年第1期59-67,共9页
Metabolic changes in rats with photochemically induced cerebral infarction and the effects of batroxobin were investigated 1, 3, 5 and 7 days after infarction by means of magnetic resonance imaging (MRI), 1H- and 31P-... Metabolic changes in rats with photochemically induced cerebral infarction and the effects of batroxobin were investigated 1, 3, 5 and 7 days after infarction by means of magnetic resonance imaging (MRI), 1H- and 31P-magnetic resonance spectroscopy (MRS). A region of T2 hyperintensity was observed in left temporal neocortex in infarction group and batroxobin group 1, 3, 5 and 7 days after infarction. The volume of the region gradually decreased from 1 day to 7 days after infarction. The ratio of NAA/Cho + Cr in the region of T2 hyperintensity in the infarction group was significantly lower than that in the corresponding region in the sham-operated group 3, 5 and 7 days after infarction respectively (P 展开更多
关键词 Animals Aspartic Acid BATROXOBIN Cerebral Infarction Magnetic Resonance Imaging Male PHOTOCHEMISTRY photosensitizing agents Random Allocation RATS Rats Sprague-Dawley Rose Bengal
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Site- and orientation-specific binding of hematoporphyrin monomethyl ether to human serum albumin revealed by single spectral kinetic parameter
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作者 张露勇 张淼 +2 位作者 邱海霞 顾瑛 赵井泉 《Journal of Chinese Pharmaceutical Sciences》 CAS CSCD 2013年第6期491-495,共5页
Interaction of a drug molecule with human serum albumin (HSA) is usually studied by fluorescence responses of the ligand or/and the single tryptophan residue (Trp-214) of the protein, but qualitative spectral info... Interaction of a drug molecule with human serum albumin (HSA) is usually studied by fluorescence responses of the ligand or/and the single tryptophan residue (Trp-214) of the protein, but qualitative spectral information may lead to multiple conclusions. In this work, we report a study on the interaction of hematoporphyrin monomethyl ether (HMME) with human serum albumin (HSA), using the environment-sensitive spectra of HMME and reaction-induced fluorescence response of Trp-214. Particularly, the single kinetic parameter, the linear slope, was derived from the concentration-dependent absorbance or fluorescence of HMME in a certain solvent. A quantitative change in the slope at [HMME]/[HSA] = 1 : 1 clearly demonstrated a specific binding of HMME to site I. The microenvironment in site I may be comparable to that in DMSO solvent, because of the similarity of the slope. Linear correlation of the fluorescence to the absorbance of HMME in site I indicates that the energy transfer is not responsible for Trp-214 fluorescence quenching but an electron transfer may be possible. In addition, much higher rate observed for the binding of HMME or 2-taurine-substituted HB (THB) with HSA than that of hypocrellin B was due to the electrostatic attraction under physiological condition. 展开更多
关键词 Human serum albumin photosensitizing agent Specific binding Dimensional fitting Electrostatic driving
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