动物血资源的利用

我国是世界上动物血资源最丰富的国家之一。据统计,每年约产猪血22万吨,牛血1万吨,羊血1.5万吨。目前除一小部分得到利用外,大部被废弃(尤其是大中城市)。大力开发利用我国的动物血资源可获得巨大的经济效益。目前,国内、外对动物血资源的利用主要有以下诸方面: 一、食品与饲料工业动物血含有丰富的蛋白质(16.4%-18.9%),其组成包括人体必需的全部八种必需氨基酸,赖氨酸和亮氨酸的含量尤高。还含有丰富的铁、钙、磷、镁、铜、锰、钾等元素,维生素(如B_(12),B_2),脂质和糖     

山 茶科濒危树种猪血木

猪血木(Euryodendron excelsum)是植物分类学家张宏达教授1963年发表的中国特有单种属植物,是山茶科中最高大的乔木树种。根据过去的调查记录,猪血木仅分布在广东省阳春县八甲乡(现为阳春市八甲镇)和广西平南和巴马等地。但随着人类对自然资源需求的增加:砍伐木材、开荒造田、建筑家园……猪血木的数量急剧下降。在广西的分布点,猪血木早已     

我国食用菌的药用研究

我国食用菌资源非常丰富,它们之中有些属于子囊菌纲(Ascomycetes),如块菌(truffles)和羊肚菇(morels);但绝大多数属于担子菌纲(Basidiomycetes),如香菇、草菇、蘑菇、银耳、木耳等。由于食用菌类含有丰富的蛋白质、维生素和碳水化合物,且味鲜可口,因此早已为人所共知的佐膳佳品。其中某些食用菌作为药用已有悠久的历史,但一直发展缓慢,只是近十几年来,应用现代新技术、深入研究食用菌的有效成分和作用机理,才使我国食用菌在药用研究上有了长足的进步。现分别将即有食用又有药用价值的菌概述如下: 一、香菇(Lentinus edodes) 香菇是营价值极为养丰富的“植物性食物”,作为营养上不可缺少的五种成分——蛋白质、脂肪、矿物质、维生素等,几乎是任何其他植物性食物不能代替的。此外钙、钠磷等无机物质以及维生素B_1、B_2、B_(12)、维生素D原(麦角甾醇)含量也相当高。香菇菌丝体细胞内还含有三十多种酶和十几种氨基酸。     

从猪血水解液中提取酸性、碱性氨基酸和亮氨酸

<正> 猪血中含有丰富的蛋白质。试验结果表明,猪血由除去大量水份外,约含20％～25％的干物质。这种干物质主要成份为蛋白质。应用猪血粉为蛋白质原料水解提取氨基酸的方法国内已见报道。我厂自1978年起开始研究直接利用猪血作为蛋白质原料水解提取酸性、碱性氨基酸和亮氨酸。经过努力,我们采用较高的流速,用732阳离子交换树脂柱将水解液中氨基酸粗略分离分组,然后利用一些氨基酸的     

拐枣的食用价值研究——Ⅰ:营养成分分析

本研究对拐枣所含营养成分,包括糖、脂类、蛋白质、维生素和人体必需无机元素进行了综合分析,结果表明,拐枣中糖、蛋白质、维生素B_1、B_2、C、胡萝卜素,K、Na、Ca、Mg、Fe含量丰富,有较高食用价值。     

应用阳离子交换树脂从猪血粉水解液中分离制备碱性氨基酸

<正> 本文介绍以猪血粉为原料应用国产强酸型732阳离子交换树脂,单柱体一次分离碱性氨基酸 L-组氨酸,L-赖氨酸,L-精氨酸;并制备其盐酸盐之新方法,适合于工业规模生产。一、前言众所周知,猪血内含有丰富的蛋白质,它可以水介成为各种氨基酸,分离猪血中氨基酸,使之为人类健康造福,是重要的科研题材之一。对于食品系统各肉联厂来说更有其重大经济价值。     

用于输送肽类及蛋白质类药物的新的药物传输系统展示出前景

澳大利亚的科学家发现了一种简单的、花费不多但行之有效的方法,用这种方法可以解决抗原或肽激素一类的蛋白质药物对人与动物的口服问题。这种方法就是使用维生素B_(12)。Biotechnology Australia P/L的Greg Russell-Jones及其同事将维生素B_(12)共价地联接到蛋白质(牛血清清蛋白和鸡γ-球蛋白)和激素(促黄体     

猪血红蛋白的酶解及氨基酸含量的研究

猪血是一种营养价值高而价格低廉的蛋白质资源.猪血中含有丰富的蛋白质,其中血红蛋白占主要部分.因此,对血红蛋白及其水解产物的研究受到了国内外众多学者的关注.为选出适合于水解猪血红蛋白的蛋白酶,笔者采用碱性蛋白酶、木瓜蛋白酶、中性蛋白酶对猪血进行单酶和复合酶水解试验,确定碱性蛋白酶为水解猪血的适用酶.通过质谱仪测定,碱性蛋白酶酶解产物分子量集中在800～2400道尔顿,而800～1260道尔顿区间占主要部分;经全自动氨基酸分析仪测出其产物含有17种氨基酸,其中含8种必需氨基酸,必需氨基酸占总氨基酸量的50.93%,说明碱性蛋白酶酶解产物是制作食品和饲料添加剂的理想资源.     

哺乳动物线粒体蛋白质翻译及其调控机制

线粒体是真核细胞内参与能量生成和物质代谢的重要细胞器。线粒体核糖体(mitochondrial ribosome, MR)作为细胞器中的翻译机器,用于表达线粒体DNA(mitochondrial DNA, mtDNA)编码的基因。近年来,随着研究的不断深入,人们对参与哺乳动物线粒体蛋白质翻译的蛋白质因子及其翻译的基本过程有了越来越清晰的认识,这对阐明线粒体蛋白质翻译的调控机制及研究人类线粒体疾病等方面具有重要的意义。线粒体蛋白质的翻译过程分为起始、延伸、终止和回收四个阶段。本文综述哺乳动物线粒体核糖体的结构与功能,以及线粒体蛋白质翻译因子的性质与功能,并进一步探讨翻译激活因子、微小RNA、线粒体COX翻译调控组装中间体(mt-translation regulation assembly intermediate of COX, MITRAC)以及核糖体的翻译后修饰对线粒体蛋白质翻译的调控及其机制,展望其对人类线粒体相关疾病研究的应用前景。     

不同发酵材料对甲烷杆菌合成维生素B_(12)的影响

维生素B_(12)也称氰钴胺素,是首先在动物性蛋白质中被发现的一种促生长因素,后来在城市下水道、污水处理厂的活性污泥和沼气残留物中被发现。无论动物或植物都不能合成维生素B_(12),它只能由某些微生物合成,如灰色链霉菌(Streptomycesgriseus)、巨大芽孢杆菌(Bacillus megaterium)、菲德力丙酸杆菌(Propionibacterium freudereichii)、舒氏丙酸杆菌(P·shermaii)等。在嫌氧发酵过程中,某些甲烷菌如欧氏甲烷杆菌(Methano bacterium omelianski)的生长,也产生维生素B_(12)。日本小野英男于1950年报道了测定酒     

氨基酸混合液脱色条件的比较选择

以四种粉末状活性炭作为脱色剂,对猪血粉水解液进行脱色比较,结果表明：江西产的４号粉末状活性炭脱色效果最佳。本文还对４号脱色炭的脱色条件进行了摸索研究。     

Calcium binding of bovine protein S. Effect of thrombin cleavage and removal of the gamma-carboxyglutamic acid-containing region

Thrombin cleaves protein S at arginine residues 52 and 70 resulting in loss of cofactor activity and reduced Ca2+ ion binding. After thrombin cleavage the NH2-terminal region containing gamma-carboxyglutamic acid (Gla) is linked to the large COOH-terminal fragment by a disulfide bond. Measurements of the rate of disulfide bond reduction by thioredoxin in intact protein S showed that the disulfide bonds are largely inaccessible to thioredoxin in the presence of Ca2+ ions, whereas in the presence of EDTA apparently all of the disulfide bonds are rapidly reduced. Probing the reactivity of the disulfide bonds in thrombin-modified proteins indicated that the thrombin cleavage induces a conformational change in the protein. After thrombin cleavage of protein S, the domain containing gamma-carboxyglutamic acid could be removed by selective reduction with thioredoxin followed by alkylation of the sulfhydryl groups. Ca2+ ion binding was compared in intact protein S, thrombin-modified protein S, and Gla domainless protein S. The intact protein S bound several Ca2+ ions, and the binding was not saturable. Thrombin-modified protein S, whether intact or with the Gla domain removed by selective reduction, bound two to three Ca2+ ions with a KD of 15-20 microM. The Gla domain in thrombin-modified protein S thus does not contribute significantly to the high affinity Ca2+ ion binding. Thrombin cleavage of protein S may be of physiological importance in the regulation of blood coagulation.     

Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains

Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade. Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion. Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI. The disulfide bonds in the carboxyl-terminal portion of the molecule were similar to those in the catalytic region of other serine proteases. The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.     

A new spectroscopic approach to examining the role of disulfide bonds in the structure and unfolding of soybean trypsin inhibitor

Although it is well-known that disulfide bonds stabilize the secondary structure of many proteins, it is difficult to directly probe both disulfide bond formation/breakage and the resulting secondary structural changes during the course of the protein folding/unfolding process. In this work, we have used a new, real-time spectroscopic approach to examine how the reduction of two disulfide bonds affects the secondary structure of soybean trypsin inhibitor (STI). The disulfide bonds are reduced with tris(2-carboxyethyl)phosphine (TCEP) at 40 degrees C, and the reduction process is probed in real-time using sulfur X-ray absorption spectroscopy. Circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopies are used concurrently to determine the structural changes caused by reduction of the disulfide bonds. Results demonstrate a noncooperative reduction of the two disulfide bonds within 5 min, likely because they are located on the surface of the protein. The unfolding of STI lags behind; dramatic changes are not observed until 60-90 min after the reduction was initiated. The CD and FTIR spectra indicate a decrease in the amount of extended (hydrated) coil, suggesting that the STI structure slowly collapses after the disulfide bonds are reduced. Thus, although the disulfide bonds are not located near the active site of STI, they play a crucial role in stabilizing the protein structure, which is necessary to sustain enzymatic activity.     

Antiparallel alignment of the two protomers of the regulatory subunit dimer of cAMP-dependent protein kinase I

The purified type I regulatory subunit of cAMP-dependent protein kinase is a dimeric protein, and the two protomers of the dimer are linked by two interchain disulfide bonds. The disulfide linkages that join these two polypeptide chains have been identified in order to provide a structural basis for the orientation of the two chains in the asymmetric dimer. Disulfide bonds were found to exist exclusively between Cys-16 and Cys-37, and this assignment, thus, establishes a general antiparallel alignment of the two chains. Two other homologous proteins, the type II regulatory subunit and the cGMP-dependent protein kinase also are dimeric proteins. In all three proteins, a relatively small, nonhomologous, amino-terminal segment of the polypeptide chain is essential for maintaining the dimeric aggregation state.     

Groups of bonds determining the configuration of the thylakoid system

Four groups of bonds determining the configuration of the thylakoid system have been established. The hypothesis presented here postulates the following. 1. There exist continuous lateral protein-protein interactions (bonds) all over the thylakoid membrane. 2. Lateral protein bonds are subdivided into two independent groups - lateral bonds of outer and inner membrane leaflets. 3. The configuration of a single thylakoid is determined by the mutual action of lateral and interlumenal bonds of the inner membrane leaflet, and the configuration of the thylakoid system of a chloroplast is determined by the mutual action of lateral and intermembrane (stacking) bonds of the outer membrane leaflet.     

The road to the first,fully active and more stable human insulin variant with an additional disulfide bond

Insulin, a small peptide hormone, is crucial in maintaining blood glucose homeostasis. The stability and activity of the protein is directed by an intricate system involving disulfide bonds to stabilize the active monomeric species and by their non‐covalent oligomerization. All known insulin variants in vertebrates consist of two peptide chains and have six cysteine residues, which form three disulfide bonds, two of them link the two chains and a third is an intra‐chain bond in the A‐chain. This classical insulin fold appears to have been conserved over half a billion years of evolution. We addressed the question whether a human insulin variant with four disulfide bonds could exist and be fully functional. In this review, we give an overview of the road to engineering four‐disulfide bonded insulin analogs. During our journey, we discovered several active four disulfide bonded insulin analogs with markedly improved stability and gained insights into the instability of analogs with seven cysteine residues, importance of dimerization for stability, insulin fibril formation process, and the conformation of insulin binding to its receptor. Our results also open the way for new strategies in the development of insulin biopharmaceuticals. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.     

Water mobility, denaturation and the glass transition in proteins

A quantitative mechanism is presented that links protein denaturation and the protein-water glass transition through an energy criterion for the onset of mobility of strong protein-water bonds. Differences in the zero point vibrational energy in the ordered and disordered bonded states allow direct prediction of the two transition temperatures. While the onset of water mobility induces the same change in heat capacity for both transitions, the order-disorder transition of denaturation also predicts the observed excess enthalpy gain. The kinetics of the water and protein components through the glass transition are predicted and compared with dielectric spectroscopy observations. The energetic approach provides a consistent mechanism for processes such as refolding and aggregation of proteins involved in protein maintenance and adaptability, as the conformational constraints of strong water-amide bonds are lost with increased molecular mobility. Moreover, we suggest that the ordered state of peptide-water bonds is induced at the point of protein synthesis and could play a key role in the function of proteins through the enhancement of electronic activity by ferroelectric domains in the protein hydration shell, which is lost upon denaturation.     

Catch-bond mechanism of force-enhanced adhesion: counterintuitive, elusive, but ... widespread?

Catch bonds are bonds between a ligand and its receptor that are enhanced by mechanical force pulling the ligand-receptor complex apart. To date, catch-bond formation has been documented for the most common Escherichia coli adhesin, FimH, and for P-/L-selectins, universally expressed by leukocytes, platelets, and blood vessel walls. One compelling explanation for catch bonds is that force-induced structural alterations in the receptor protein are allosterically linked to a high-affinity conformation of its ligand-binding pocket. Catch-bond properties are likely to be widespread among adhesive proteins, thus calling for a detailed understanding of their underlying mechanisms and physiological significance.