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文献检索课综合检索报告姓名 __代小慧_______ 班级 ___食品02____学号 __07060080202_________检索课题（中文） ____蛋白质测定与分析_____________________ （英文）____ protein _ determine and_ analysis _一、检索策略检索词：主题词（中文）___蛋白质_____ （英文）__ protein______ 相关词：（中文）_牛奶______ （英文）___milk_____副主题词：（中文）_测定分析_______ （英文）_ determine_ analysis ____二、检索结果：中文期刊刊名：《粮食科技与经济》篇名：粮食中粗蛋白质2种测定方法的比对分析作者：李梅2008年6期摘要:采用凯氏微量定氮法和定氮仪法测定粮食中的粗蛋白质，并对结果进行比对分析，结果表明定氮仪法操作简单、准确、稳定、省时、安全，完全能够达到粮食检测技术要求。

2刊名:《中国公共卫生》篇名：食品中蛋白质纳氏剂法快速测定作者：彭科怀廖应萍赵年华2008年24卷4期摘要：目前食品中蛋白质的测定方法有蛋白质自动分析仪，近红外自动测定仪，紫外分光光度法以及凯氏定氮法等。

本文采用纳氏试剂作为显色剂测定食品中蛋白质含量，适用范围广，可用于各类食品及保健食品的检测。

用本法对标准品、质控样品进行测定获得满意结果．对批量样品的快速测定更具有实用性。

现将结果报告如下。

3刊名：《分析化学》篇名：流动注射光度法测定黄酒中蛋白质的含量和分子量分布作者：林峰白少勇2005年33卷10期摘要:将流动注射技术引入Bradford蛋白质测定法，利用Sepadex G-100凝胶层析柱分离黄酒中的蛋白质，可直接测定蛋白质的含量和分子量分布。

成品酒（熟酒）为5．32g/L（6．86g ／L）；高分子蛋白质（Fw〉25000）占10．52％（13、08％）；中分子蛋白质（FW：25000～5000）占49、12％（54．12％）；小分子蛋白质（FW〈5000）占40、36％（32、80％），并得到黄酒中蛋白质含量与分子量分布的曲线谱图，可监控和预测黄酒的品质。

4 刊名：《江西化工》篇名：蛋白质测定方法比较与研究进展作者：乐萍雷颉熊建铭2007年2期摘要：蛋白质是生物体中含量最高,功能最重要的生物大分子,与生命的起源和进化都密切相关,因此蛋白质也是生命科学中极为重要的研究对象.关于蛋白质的分析研究,一直是化学家及生物学家极为关注的问题,其含量的测定在生化分析和临床分析中具有重要意义,研究和开发新的、高灵敏度的蛋白质测定方法是生物化学研究的一个活跃领域本文综述了近年来蛋白质测定的方法的研究进展,包括分光光度法、双缩脲法、凯氏定氮法、电泳分析法、质谱分析法在蛋白质测定中的应用.总结各种方法的特点及适用条件.质谱分析是测定结果最准确的测定方法;凯氏定氮法适用范围最广泛,分光光度法是最为简便快速的测定方法.5刊名：《苏州大学学报：自然科学版》篇名：用考马斯亮蓝测定植物粗提液中可溶性蛋白质含量方法的研究作者：曲春香沈颂东王雪峰崔永华宋卫平2006年22卷2期摘要：用木立芦荟的叶片为材料,以牛血清白蛋白为参照,对蛋白质与考马斯亮蓝G-250结合后的光吸收稳定性,不同的蛋白质溶剂、植物粗提液等对光吸收的影响进行了研究.结果表明：蛋白质与考马斯亮蓝结合后,在595nm处的光吸收值不很稳定,通过降低仪器的灵敏度可以提高光吸收的稳定性;以0.02～0.5mol·L^-1pH为6.8的磷酸缓冲液、0.1～1.0 mol·L^-1pH为6.8的Tris-HCI缓冲液为蛋白质溶剂,对蛋白质与考马斯亮蓝结合后的线性无影响;芦荟叶片粗提液中的其他成分对其中可溶性蛋白质与考马斯亮蓝结合后的线性亦无显著影响2、外文期刊1．Title: Novel UV assay for protein determination and the characterization of copper-protein complexes by mass spectrometryAuthors:Drochioiu.G ；Damoc.N.E ；Przybyiski.M 2006 V 69 L3 Abstract：A very simple, highly selective and sensitive assay of proteins based on the biuret absorption in the ultraviolet region has been developed. The well-known biuret assay is based on the reaction of proteins with copper ions under strong alkaline conditions to form a copper-protein complex. Yet, copper ions may seriously interfere with the determination if the measurement is made in the UV range. In the present approach, proteins mobilize copper ions from insoluble salts at different pH values, and the copper-protein complexes are investigated by UV spectrophotometry and mass spectrometry. Upon using copper phosphate, free copper ions do not interfere with the determination from 540 to 240 nm. Copper absorbance slowly increases from 240 to 190 nm where a blank with the reagents is recommended. A maximum absorbance for the copper-protein complex was found at 226 nm and high pH value.The stoichiometries of the copper-protein complexes measured directly with a mass spectrometer are pH dependent: half of the peptides without any histidine residue chelate just a single Cu2+ ion at pH 7.4 but each such peptide mobilizes from 1 to 6 Cu2+ ions at pH 10.3. To determine proteins, 1-1.5 ml of 1.8% KOH solution with 0-20 μg ml-1 protein is treated with 25 mg of copper phosphate powder. The mixture is powerfully stirred, centrifuged, and the absorbance of the supernatant is measured at 226 nm in 1 cm quartz cuvettes against a blank of the reagents. The color system obeys Beer's law in the range 0.1-20 μg ml-1 protein at this wavelength. The molar absorptivity value proved to be a characteristic of each protein being analyzed. Therefore, individual proteins should be used to plot calibration curves. This assay proved to be over 100 times more sensitive than the classical biuret procedure. The method is highly selective and the determination is little affected by the presence of other substances. All other important analytical parameters were studied and practical applicability of the method has been verified by the analysis of some biological materials. © 2005 Elsevier B.V. All rights reserved.2．Title：Determination of protein and gossypol content in cotton kernel powder with near infrared reflectance spectroscopyAuthors：Qin Li；Shen Xiao-Jia；Chen Jin-Hong；Zhu Shui-Jin 2010 V30 L3 Abstract：Near-infrared reflectance spectroscopy (NIRS) was used as a rapid and nondestructive method to determine the protein content and gossypol content in cotton kernel powder samples, using 49 upland cotton (Gossypium hirsutum L.) germplasms and 188 recombinant inbred lines (RILs). The cottonseed samples harvested from the upland cotton germplasms and RILs grown in different cotton growing regions in different years were analyzed chemically for protein and gossypol contents, as well as scanned in the reflectance mode of a scanning monochromator. Using ISI software for scanning and data analysis, protein and gossypol calibration equations were obtained with a standard normal variate + detrending scatter correction and a 2, 4, 4, 1 math treatment and modified partial least square (MPLS) as the regression method. The protein content calibration results revealed that the multiple correlation coefficients (RSQ) and statistic 1-variance ratio (1-VR) for the determination of protein content in cottonseed kernels were 0.933 and 0.929, respectively, and its standard error of calibration (SEC) and standard error of cross validation (SECV) were 0.623 and 0.638, respectively. As the calibration equations were judged by the calibration RSQ (or 1-VR) and SEC (or SECV), the results indicated that NIRS is comparable to chemical methods in both accuracy and prediction and is reliable in the determination of protein content in cottonseed kernels. However, the RSQ, SEC, 1-VR and SECV for gossypol content determination of NIRS were 0.836, 0.811, 0.074 and 0.079, respectively. Although it was weaker than that of protein content, the NIRS method is still good enough for the determination and prediction of the gossypol content in cottonseed kernels. Therefore, NIRS models were successfully developed for protein content and gossypol content analysis ofcotton kernel powder sample in the present study and they could be introduced into the cotton germplasm evaluation and breeding program for the cottonseed quality improvement.3 Title：Towards protein interaction analysis through surface labeling Author：Cantoni.Virqinio；Gatti.Riccardo；Lombardi.Luca2009 V 5716LNCS Abstract：The knowledge of the biological function of proteins would have great impact on the identification of novel drug targets, and on finding the molecular causes of diseases. Unfortunately, the experimental determination of protein function is a very expensive and time consuming process. As a consequence, the development of computational techniques to complement and guide the experimental process is a crucial and fundamental step for biological analysis. The final goal of the activity here presented is to provide a method that allows the identification of sites of possible protein-protein and protein-ligand interaction on the basis of the geometrical and topological structure of protein surfaces. The goal is then to discover complementary regions (that is with concave and convex segments that match each others) among different proteins. In particular, we are considering the first step of this process: the segmentation of the protein surface in protuberances and inlets through the analysis of convexity and concavity. To this end, two approaches will be described with a comparative assessment in terms of accuracy and speed of execution. © 2009 Springer Berlin Heidelberg.3、学位论文蛋白质与荧光探针的作用及其分析应用研究作者：冯艳花学位授予单位：河南师范大学摘要：蛋白质是生命最重要的物质基础之一，其定量测量是化学、生物化学、医学等研究领域的重要课题。