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131.
柱后衍生-荧光检测高效液相色谱法快速测定鲜牛奶中链霉素残留量 总被引:21,自引:0,他引:21
牛奶样品经磷酸溶液提取,提取液用苯磺酸阳离子交换柱和C18固相萃取柱净化,链霉素残留液用甲醇从C18固相萃取柱上洗脱,经旋转蒸发器减压蒸干,残渣用0.01mol/L庚烷磺酸钠溶液溶解,用柱后衍生-高效液相色谱荧光检测器在激发波长263nm和发射波长435nm测定.方法线性范围为0.01~0.10mg/kg;在0.01~0.10mg/kg范围,三个添加水平的回收率为78.3%~80.2%,变异系数(CV)为7.4%~12.4%,方法检出限为0.005mg/kg. 相似文献
132.
van de Waterbeemd H Smith DA Jones BC 《Journal of computer-aided molecular design》2001,15(3):273-286
Lipophilicity, often expressed as distribution coefficients (log D) in octanol/water, is an important physicochemical parameter influencing processes such as oral absorption, brain uptake and various pharmacokinetic (PK) properties. Increasing log D values increases oral absorption, plasma protein binding and volume of distribution. However, more lipophilic compounds also become more vulnerable to P450 metabolism, leading to higher clearance. Molecular size and hydrogen bonding capacity are two other properties often considered as important for membrane permeation and pharmacokinetics. Interrelationships among these physicochemical properties are discussed. Increasing size (molecular weight) often gives higher potency, but inevitably also leads to either higher lipophilicity, and hence poorer dissolution/solubility, or to more hydrogen bonding capacity, which limits oral absorption. Differences in optimal properties between gastrointestinal absorption and uptake into the brain are addressed. Special attention is given to the desired lipophilicity of CNS drugs. In examples using -blockers, Ca channel antagonists and peptidic renin inhibitors we will demonstrate how potency and pharmacokinetic properties need to be balanced. 相似文献
133.
Present proteomics and biomedicine require sensitive analytical methods for all proteins. Recent progress in electrochemical analysis of peptides and proteins based on their intrinsic electroactivity is reviewed. Tyrosine and/or tryptophan‐containing proteins are oxidizable at carbon electrodes. At mercury electrodes all peptides and proteins (about 13 peptides and >25 proteins were tested) produce chronopotentiometric peak H at nanomolar concentrations. This peak is sensitive to changes in protein structure. Microliter sample volumes are sufficient for the analysis. Electrochemical methods can be used in studies of nucleic acid‐protein interactions and can be applied in biomedicine. Examples of such applications in neurogenerative diseases and cancer are presented. 相似文献
134.
Alessandra Sussulini Jerusa S. Garcia Márcia F. Mesko Diogo P. Moraes Érico M. M. Flores Carlos A. Pérez Marco A. Z. Arruda 《Mikrochimica acta》2007,158(1-2):173-180
Two methods of protein extraction for soybean seeds were evaluated in terms of preservation of the metal ions bound to proteins
after the extraction and separation procedures. The proteins were firstly separated according to their molar masses by polyacrylamide
gel electrophoresis. Then, the protein bands were mapped by synchrotron radiation X-ray fluorescence in order to establish
which metal ions were present in each one. Finally, some mapped protein bands were decomposed by microwave-assisted combustion
and Ca, Cu, K, Mg, Mn, and Zn were quantified by inductively coupled plasma mass spectrometry or inductively coupled plasma
optical emission spectrometry. The extraction methods studied were Method A (based on the treatment of ground soybean seeds with hexane and their extraction with Tris–HCl and β-mercaptoethanol) and
Method B (based on the treatment of ground soybean seeds with petroleum ether and their extraction with Tris–HCl, dithiothreitol,
phenylmethanesulfonyl fluoride, sodium dodecyl sulfate and potassium chloride). The best method was Method B, in which a 78% higher extraction efficiency was obtained when compared to Method A. Additionally, the metal-protein interactions were more appropriately preserved when Method B was applied, where the most affected ions were those that are bound weakly to proteins, such as Ca, K, and Mg. 相似文献
135.
Volkhard Helms 《Chemphyschem》2007,8(1):23-33
Proteins are key components of biological cells. For example, enzymes catalyze biochemical reactions, membrane transporters are responsible for uptake and release of critical and superfluous components from the cell environment, and structural proteins are responsible for the stability of the cell wall and cytoskeleton. Many of the diverse protein functions involve dynamic transitions ranging from small local atomic displacements up to large allosteric conformational changes. In any conformation, proteins are in contact with the universal solvent medium of cells, water. Water not only surrounds proteins but is often an integral part of proteins and also is involved in key mechanistic steps. This Minireview discusses recent experimental and theoretical results on the role of water for protein dynamics and function. 相似文献
136.
Thazha P PrakashAndrew M Kawasaki Elena A LesnikNamir Sioufi Muthiah Manoharan 《Tetrahedron》2003,59(37):7413-7422
Synthesis of a series of 2′-O-[2-[(N,N-dialkylamino)oxy]ethyl]-modified 5-methyluridine nucleoside phosphoramidites and solid supports are described. Using these monomers, modified oligonucleotides containing phosphodiester linkages were synthesized in high yields. These modified oligonucleotides showed enhanced binding affinity to the complementary RNA (and not to DNA) and excellent nuclease stability with t1/2>24 h. The human serum albumin binding properties of modified oligonucleotides have been evaluated to assess their transport and toxicity properties. 相似文献
137.
C. Jolicoeur B. Riedl D. Desrochers L. L. Lemelin R. Zamojska O. Enea 《Journal of solution chemistry》1986,15(2):109-128
The limiting partial molar volumes V
o
and heat capacities C
p
o
of 20 amino acids have been determined in water and in 8 molar urea at 25.0°C using flow calorimetry and flow densimetry. The side chain contributions to V
o
and C
p
o
were obtained as the difference between the properties of the various amino acids and those of glycine, both in water and in 8M urea. The solvent accessible surface area of the amino acid residues were obtained using a method developed by Hermann, and the total surface areas were separated into their hydrophobic A
Hb
and hydrophilic components. In water, C
p
o
values for the various residues C
p
o
(R) were found well correlated with A
Hb
, though much less so in the urea solution. Hence, C
p
o
(R) values, in water yield a good estimate of side chain hydrophobicity, but the (waterurea) transfer heat capacities appear strongly affected by specific solvation effects in the urea solution.Presented at the sixth Italian meeting on Calorimetry and Thermal Analysis (AICAT) held in Naples, December 4–7, 1984. 相似文献
138.
139.
140.
Sun Y Irie M Kishikawa N Wada M Kuroda N Nakashima K 《Biomedical chromatography : BMC》2004,18(8):501-507
A highly sensitive HPLC method was developed for the determination of xenoestrogenic compound, bisphenol A (BPA) in human breast milk samples. After a two-step liquid-liquid extraction, BPA was derivatized with fluorescent labeling reagent, 4-(4,5-diphenyl-1H-imidazol-2-yl)benzoyl chloride (DIB-Cl). The excess fluorescent reagent could be removed effectively using a column-switching system. The separation of DIB-BPA from endogenous materials in milk was carried out on two C(18) columns and fluorescence intensity was monitored at 475 nm with the excitation of 350 nm. A good linearity (r = 0.994) was observed of BPA in the concentration range of 0.2-5.0 ng mL(-1) in breast milk, and the detection limit was 0.11 ng mL(-1) at a signal-to-noise ratio of 3. Intra- and inter-day precision (RSD, %) were less than 8.7 and 10.4, respectively. Twenty-three breast milk samples of healthy lactating women were analyzed for the BPA concentration; the mean value was 0.61 +/- 0.20 ng mL(-1), with no correlation to the lipid content of milk samples. 相似文献