利用中华稻蝗粉饲养鹌鹑试验研究

昆虫蛋白质的开发利用是当前值得深入研究的课题。本文以中华稻蝗粉做为动物蛋白源,代替秘鲁鱼粉饲养鹌鹑,对比了两种动物蛋白源对鹌鹁生长发育的影响。稻蝗粉的粗蛋白质的含量与秘鲁鱼粉相等,16种氨基酸的总含量略低,磷、钙、脂肪的含量只是鱼粉的1/4、1/19、1/2左右。用等量稻蝗粉和鱼粉配制的饲料,分别对两组鹌鹑进行饲养实验,结果证明,用稻蝗粉做动物蛋白源,能使鹌鹑正常发育,翅的生长速度比秘鲁鱼粉组快,但日产蛋量比秘鲁鱼粉组略低,成熟期比秘鲁鱼粉组晚10天。     

蛋白核小球藻粉的蛋白质、氨基酸含量及营养价值评价

对蛋白核小球藻粉主要营养成分的分析结果表明,其蛋白质含量为63.60%,18种氨基酸总量为55.95%,8种必需氨基酸含量为23.35%,氨基酸分(AAS)为64.3,蛋氨酸+胱氨酸为第一限制性氨基酸。小球藻粉营养成分全面,是优良的单细胞蛋白源。     

蛋白核小球藻粉中氨基酸含量及饲用价值分析

测定了蛋白核小球藻粉的蛋白质含量及18种氨基酸组分,用氨基酸分(AAS)、必需氨基酸指数(EAAI)等指标对蛋白核小球藻粉氨基酸营养进行评价。结果表明：蛋白核小球藻粉粗蛋白和必需氨基酸含量高,是一种优良的饲料蛋白源。     

三种哺乳动物初乳乳汁氨基酸含量的比较

采用高效液相色谱法分析了人、牛、猪3种哺乳动物的初乳乳汁中氨基酸含量,结果表明:谷氨酸的含量在3种哺乳动物的初乳乳汁中是最高的,而蛋氨酸的含量最低;从3种动物比较来看,猪乳与牛乳的氨基酸含量比较接近,而人乳与其他两种动物有较大的差异.     

祁连山区几种草地蝗虫蛋白质营养评价

为评价草地蝗虫作为家禽蛋白源饲料的营养价值.本研究以几种草地蝗虫为供试对象,在分析测定其蛋白和氨基酸含量基础上,采用国际通用蛋白质营养评价标准,分析评价其蛋白质营养价值.结果表明,草地蝗虫蛋白含量高(62.4%～67.3%,DM),氨基酸组分齐全、家禽所需必需氨基酸约占蝗虫总干重的30.3%～34.2%,其氨基酸模式优...     

五种啮齿类动物mtDNA蛋白编码基因序列变化的比较

目的利用本实验室测定的中国地鼠、金黄地鼠和GenBank中田鼠、小鼠、大鼠的线粒体全基因组序列,比较分析五种啮齿类动物的mtDNA蛋白编码基因序列的变异,探讨其分子进化关系。方法将五种动物各自的13个蛋白编码基因分别连接成一个序列,用DNAstar-EditSeq分析软件计算每个序列的碱基长度和组成,计算蛋白编码基因的碱基和氨基酸的差异。以人为外群,基于连接在一起的13个蛋白编码基因的氨基酸序列,用MEGA4.0软件通过最大简约性法(MP)和非加权成对平均数法(UPGMA)构建进化树。结果在五种啮齿动物的13个蛋白基因序列中,A、T、C、G碱基的平均含量为32.4%、29.6%、26.2%和11.9%,中国地鼠mtDNA各蛋白编码序列以及其编码的氨基酸序列与其他物种相比,与金黄地鼠的相应序列差异最小,与大鼠mtDNA各蛋白编码序列以及其编码的氨基酸序列差异较大。分子进化树也显示中国地鼠和金黄地鼠的亲缘关系最近,与小鼠、大鼠存在的差异相对大。结论五种动物的碱基组成的百分比中显示G的相对缺乏,相互之间的进化关系与传统的分类地位基本吻合。     

白颈环毛蚓(Pheritima catifornica)与壮伟环毛蚓(Amynthas robusto)的PTC-氨基酸分析

对白颈环毛蚓与壮伟环毛蚓的体壁及内脏器官ＰＴＣ—氨基酸的含量进行了初步分析,结果表明：两种蚯蚓具有１５种氨基酸,８种必需氨基酸含量均较高。而壮伟环毛蚓的必需氨基酸总量均超过白颈环毛蚓,也大大超过国产或进口鱼粉氨基酸总含量;加上壮伟环毛蚓个体大,分布广,又耐污染,抗病能力强,所以这是一种值得开发的动物蛋白的新资源。     

脱脂玉米胚芽营养粉与氨基酸的研究

本文提出了利用玉米胚芽制成脱脂胚芽营养粉的方法,其中着重比较了分别用乙醇和不同浓度石灰水作为脱脂浸泡剂,对成品中氨基酸含量的影响。并全分面析了脱脂玉米胚芽营养粉中氨基酸的种类与含量,认为它是一种比较理想的人类食用优质蛋白源。     

三个茯苓材料氨基酸与蛋白质的含量比较

目的：3个茯苓品种的蛋白质与氨基酸含量比较。方法：凯氏定氮法和考马斯亮蓝测定蛋白质和氨基酸含量;结果：3个品种的茯苓所含蛋白质、氨基酸种类齐全,辐射一号中人体所需的8种必需氨基酸含量最具明显优势,其游离氨基酸和总蛋白含量高于湘靖28,蛋白质与游离氨基酸含量高低为野生型＞辐射一号＞湘靖28;结论：辐射一号是一个经济价值指标较优的品种,对茯苓新品种选育和茯苓蛋白类保健品开发具有指导意义。     

L-色氨酸

<正> L-色氨酸是Hopkins和Kole于1901年发现和分离出来的氨基酸。它是一个含吲哚基的芳香族氨基酸。其化学名称为α-氨基—β-吲哚丙酸。在天然蛋白质中,一般含量甚低。含量较高的蛋、奶、肉类等动物蛋白仍不超过1%,植物蛋白中含量一般很低。特别在玉米、木茨、葫萝卜中,色氨酸含量几乎测不出来。此外,还以一些衍生物存在于自然界,如:可可的干酪苦味就是与     

Body composition of animals treated with partitioning agents: implications for human health.

Excess fat in meat products has been identified as a dietary problem by public health officials. The meat animal industry has responded during the last 25 years to concerns about excess fat intake from animal products by implementing strategies to depress fat deposition and increase lean (protein) tissue gain in meat animals. The most successful strategy to date is the use of large, late-maturing animals for meat production. At desired market weights, these animals are much leaner than smaller, early-maturing animals. In addition, exogenous agents such as anabolic steroids (FDA approved for cattle) have been used to increase lean gain and depress fat deposition in cattle. Growth hormone (GH) and beta-adrenergic agonists (beta AA) are not yet approved by the FDA, but if/when approved would also markedly increase lean gain and depress fat deposition. Both GH and beta AA are called partitioning agents because they partition nutrients and energy toward lean (protein) accretion and dramatically lower fat deposition. Contingent on approval by the FDA and subsequent adoption of partitioning agents by the animal industry would result in meat products containing less and 30% of total calories from fat.     

Changes in the Composition and Size Distribution of Soymilk Protein Particles by Heating

The protein particles in soymilk were fractionated in size by differential centrifugation. Particles of more than 100 nm in diameter (LSP) constituted 40% of the total protein in raw soymilk, 70% of the protein components being 11S globulin. LSP was not formed in the presence of 2-mercaptoethanol and sodium ascorbate. LSP was decreased by heating, and particles of 100–40 nm in diameter (MSP) were increased. The formation of MSP was not due to any degradation of LSP but to the combination of supernatant proteins of less than 40 nm in diameter with each other. MSP formed by heating contained the β subunit of 7S and the basic subunit of 11S as main components. The particles of more than 40 nm in diameter (LSP + MSP) constituted 50% of the total protein in both raw soymilk and soymilk.     

Amino acid sequence variations in protein AA of cats with high and low incidences of AA amyloidosis

1. Amyloid isolated from the liver of a domestic short-haired (DSH) cat was dissolved and purified by gel filtration for amino acid sequence analysis. 2. Sequences of two major peptides corresponding to positions 18-23 and 25-75 of human amyloid protein AA were obtained when cyanogen bromide-cleaved protein was applied to an amino acid sequenator. 3. Comparison of these regions of amyloid protein from the Abyssinian cat (high incidence of AA amyloidosis) and DSH cat (low incidence of AA amyloidosis) revealed three amino acid differences, two of which occurred within regions that are completely conserved in the Abyssinian cat and all other species. 4. Secondary prediction plots showed less potential for amyloidogenicity (i.e., less beta-sheet conformation) in protein AA of the DSH cat as compared to the Abyssinian cat and other animal species. 5. These differences in protein AA of the DSH cat may, therefore, be linked to the comparatively uncommon occurrence of AA amyloidosis in the DSH cat as compared to the Abyssinian cat and other animals species.     

Use of Life Cycle assessment in the procedure for the establishment of environmental criteria in the catalan ECO-label of leather

Life Cycle Assessment (LCA) has been used to detect the environmental ‘hot spots’ in the chrome-tanned bovine leather industry. We have studied those stages in the life cycle of leather, which occur ‘from cradle to gate’. The production chain studied starts with the agricultural products (fertiliser and pesticide production is also included) needed for cattle raising, it is followed by the slaughterhouse, and ends at the tanning industry gate. Main chemicals and waste flows in and out of this chain have also been included in the analysis. One of the main conclusions is that the tannery is an important stage in most of the impact categories, mainly due to the landfilling of the tannery wastes. Agriculture and — to a lesser extent — cattle raising also play a very important role in most of the impact categories; the former, due to the related energy consumption and use of fertilisers, and the latter due to the emissions associated with animal care. The Autonomous Government of Catalonia is using the results of this study to establish the environmental criteria that a leather product must fulfil in order to attain the Catalan eco-label.     

The lymphocyte-specific protein LSP1 binds to F-actin and to the cytoskeleton through its COOH-terminal basic domain

The lymphocyte-specific phosphoprotein LSP1 associates with the cytoplasmic face of the plasma membrane and with the cytoskeleton. Mouse LSP1 protein contains 330 amino acids and contains an NH2-terminal acidic domain of approximately 177 amino acids. The COOH-terminal half of the LSP1 protein is rich in basic residues. In this paper we show that LSP1 protein which is immunoprecipitated with anti-LSP1 antibodies from NP-40-soluble lysates of the mouse B-lymphoma cell line BAL17 is associated with actin. In vitro binding experiments using recombinant LSP1 (rLSP1) protein and rabbit skeletal muscle actin show that LSP1 binds along the sides of F-actin but does not bind to G-actin. rLSP1 does not alter the initial polymerization kinetics of actin. The highly conserved COOH-terminal basic domains of mouse and human LSP1 share a significant homology with the 20-kD COOH-terminal F-actin binding fragment of caldesmon. A truncated rLSP1 protein containing the entire COOH-terminal basic domain from residue 179 to 330, but not the NH2-terminal acidic domain binds to F-actin at least as well as rLSP1. When LSP1/CAT fusion proteins are expressed in a LSP1-negative T-lymphoma cell line, only fusion proteins containing the basic COOH-terminal domain associate with the NP-40-insoluble cytoskeleton. These data show that LSP1 binds F-actin through its COOH-terminal basic domain and strongly suggest that LSP1 interacts with the cytoskeleton by direct binding to F-actin. We propose that LSP1 plays a role in mediating cytoskeleton driven responses in lymphocytes such as receptor capping, cell motility, or cell-cell interactions.     

Crocodile farming and conservation,the example of Zimbabwe

Crocodile farming is an important and lucrative activity in Zimbabwe which provides meat for human consumption and skins for the luxury leather industry. Because it gives an economic value to this otherwise unfriendly animal, farming crocodiles has a positive side effect on the conservation of this species in the wild. This paper gives an overview of the crocodile industry in Zimbabwe.     

SopE acts as an Rab5-specific nucleotide exchange factor and recruits non-prenylated Rab5 on Salmonella-containing phagosomes to promote fusion with early endosomes

Rab-GTPase regulates the fusion between two specific vesicles. It is well documented that, for their biological function, Rab proteins need to be prenylated for attachment to the vesicle membrane. In contrast, we showed in the present investigation that SopE, a type III secretory protein of Salmonella, translocates onto Salmonella-containing phagosomes (LSP) and mediates the recruitment of non-prenylated Rab5 (Rab5:DeltaC4) on LSP in GTP form. Simultaneously, SopE present in infected cell cytosol acts as an Rab5-specific exchange factor and converts the inactive Rab-GDP to the GTP form. The non-prenylated Rab5 subsequently promoted efficient fusion of LSP with early endosomes. This is the first demonstration that a prenylation-deficient Rab protein retains biological activity and can promote vesicle fusion, if it is recruited on the membrane by some other method.     

A new lymphocyte-specific gene which encodes a putative Ca2+-binding protein is not expressed in transformed T lymphocyte lines

The LSP1 gene is a new lymphocyte-specific gene which is expressed in normal mouse B and T lymphocytes and in transformed B cells but not (or in much smaller amounts) in nine T lymphoma lines tested. No LSP1 mRNA is found in myeloid cells or in liver, kidney, or heart tissue. Inspection of the predicted LSP1 protein sequence reveals the presence of two putative Ca2+-binding domains in the LSP1 protein. Southern blotting analysis of genomic DNA from mouse liver suggests that the LSP1 gene is present as one copy per haploid genome. Similar analysis of genomic DNA extracted from three transformed B cell lines and five transformed T cell lines shows that the absence of LSP1 mRNA in T cell lines is not due to deletion or gross rearrangements of the LSP1 locus. With the use of the mouse LSP1 cDNA as a probe we can detect a cross-hybridizing RNA species in four normal human functional T cell lines but not in three transformed human T cell lines. This suggests that at least part of the DNA sequence and the expression pattern of the LSP1 gene is conserved between mouse and man. These conserved features, together with the particular expression pattern and the protein sequence homologies, suggest that the LSP1 protein is involved in a Ca2+-dependent aspect of normal T cell growth.     

Lymphocyte-specific Ca2+-binding protein LSP1 is associated with the cytoplasmic face of the plasma membrane.

The gene for LSP1 is a lymphocyte-specific gene previously isolated by us using a subtractive hybridization technique. LSP1 mRNA is found in normal and transformed B lymphocytes and in normal T lymphocytes but not in transformed T lymphocytes. To study the expression of the mouse LSP1 protein, we prepared a polyclonal antiserum specific for the LSP1 protein. Here we report that the gene for LSP1 was expressed in transformed B-lymphoma cell lines and in normal mouse thymocytes as a protein doublet with apparent molecular masses of 52 and 50.5 kilodaltons when analyzed on a sodium dodecyl sulfate-10% polyacrylamide gel. BW5147 cells transfected with an LSP1 cDNA clone expressed only the 52-kilodalton protein. No LSP1 protein was expressed in nine T-lymphoma cell lines tested. Immunofluorescence studies of intact and permeabilized cells and subcellular fractionation experiments showed that the LSP1 protein was associated with the cytoplasmic side of the plasma membrane in transformed B-lymphoma cell lines and in normal thymocytes. Using a simple filter-binding assay, we showed that recombinant LSP1 protein was Ca2+ binding, as predicted on the basis of its deduced amino acid sequence. On the basis of the particular expression pattern, the subcellular localization, and the Ca2+-binding property of the LSP1 protein, we hypothesize that the LSP1 protein is a lymphocyte-specific component of a signal transduction pathway involved in the regulation of lymphocyte growth.     

Human and mouse LSP1 genes code for highly conserved phosphoproteins

With use of the mouse LSP1 cDNA we isolated a human homologue of the mouse LSP1 gene from a human CTL cDNA library. The predicted protein sequence of human LSP1 is compared with the predicted mouse LSP1 protein sequence and regions of homology are identified in order to predict structural features of the LSP1 protein that might be important for its function. Both the human and mouse LSP1 proteins consist of two domains, an N-terminal acidic domain and a C-terminal basic domain. The C-terminal domains of the mouse and human LSP1 proteins are highly conserved and include several conserved, putative serine/threonine phosphorylation sites. Immunoprecipitation of LSP1 protein from 32P-orthophosphate-loaded cells show that both the mouse and human LSP1 proteins are phosphoproteins. The sequences of the putative Ca2(+)-binding sites present in the N-terminal domain of the mouse LSP1 protein are not conserved in the human LSP1 protein; however, a different Ca2(+)-binding site may exist in the human protein, indicating a functional conservation rather than a strict sequence conservation of the two proteins. The expression of the human LSP1 gene follows the same pattern as the expression of the mouse LSP1 gene. Southern analysis of human genomic DNA shows multiple LSP1-related fragments of varying intensity in contrast to the simple pattern found after similar analysis of mouse genomic DNA. By using different parts of the human LSP1 cDNA as a probe, we show that most of these multiple bands contain sequences homologous to the conserved C-terminal region of the LSP1 cDNA. This suggests that there are several LSP1-related genes present in the human genome.