《病毒学报》来稿需注意的一些常用规范

常用斜体规范:统计学符号:根据国家标准GB3358-82《统计名词及符号》的规定,样本的算术平均数用英文小写斜体x表示,标准差用英文小写斜体s表示,t检验用英文小写斜体t表示,F检验用英文大写斜体F表示,卡方检验用希腊字母小写斜体χ2表示,相关系数用英文小写斜体r表示,自由度用希腊字母小写斜体γ表示,概率用英文大写斜体Ρ表示,样本数用英文小写斜体n表示。基因符号通常用小写斜体,该基因表达产物用大写正体,基因位点用正体大写,突变或等位基因的符号或数字也用正体,     

科技论文正体和斜体的书写规范

统计学符号常用统计学符号一般用斜体。样本的算术平均数用英文小写x,不用大写X,也不用Mean;标准差用英文小写s,不用SD;标准误用英文小写sx,不用SE;t检验用英文小写t;F检验用英文大写F;卡方检验用希文小写χ2;相关系数用英文小写r;样本数用英文小写n;概率用英文大写P;自由度用英文小写v。     

科技论文正体和斜体的书写规范

统计学符号常用统计学符号一般用斜体。样本的算术平均数用英文小写x,不用大写X,也不用Mean;标准差用英文小写s,不用SD;标准误用英文小写sx,不用SE;t检验用英文小写t;F检验用英文大写F;卡方检验用希文小写χ^2;相关系数用英文小写r;样本数用英文小写n;概率用英文大写P;自由度用英文小写v。     

科技论文正体和斜体的书写规范

统计学符号常用统计学符号一般用斜体。样本的算术平均数用英文小写x,不用大写X,也不用Mean;标准差用英文小写s,不用SD;标准误用英文小写sx,不用SE;t检验用英文小写t;F检验用英文大写F;卡方检验用希文小写χ2;相关系数用英文小写r;样本数用英文小写n;概率用英文大写P;自由度用英文小写v。     

《病毒学报》来稿需注意的一些常用规范

正常用斜体规范:统计学符号:根据国家标准GB3358-82《统计名词及符号》的规定,样本的算术平均数用英文小写斜体x表示,标准差用英文小写斜体s表示,t检验用英文小写斜体t表示,F检验用英文大写斜体F表示,卡方检验用希腊字母小写斜体2χ表示,相关系数用英文小写斜体r表示,自由度用希腊字母小写斜体γ表示,概率用英文大写斜体Ρ表示,样本数用英文小写斜体n表示。     

《病毒学报》来稿需注意的一些常用规范

常用斜体规范:统计学符号:根据国家标准GB3358-82《统计名词及符号》的规定,样本的算术平均数用英文小写斜体x表示,标准差用英文小写斜体s表示,t检验用英文小写斜体t表示,F检验用英文大写斜体F表示,卡方检验用希腊字母小写斜体χ2表示,相关系数用英文小写斜体r表示,自由度用希腊字母小写斜体γ表示,概率用英文大写斜体Ρ表示,样本数用英文小写斜体n     

论文中统计学符号书写规则

统计学符号一般用斜体。本刊常用统计学符号介绍如下,希望作者参照执行。样本的算术平均数用英文小写x,不用大写X,也不用Mean。标准差用英文小写s,不用SD。标准误用英文小写s x,不用S E。t检验用英文小写t。F检验用英文大写F。卡方检验用希文小写χ2。相关系数用英文小写r。样本数用英文小写n。概率用英文大写P。     

稿件书写规范

论文中统计学符号书写规则统计学符号一般用斜体。本刊常用统计学符号介绍如下,希望作者参照执行。样本的算术平均数用英文小写x,不用大写X,也不用Mean。标准差用英文小写s,不用SD。标准误用英文小写xs,不用SE。t检验用英文小写t。F检验用英文大写F。卡方检验用希文小写χ2。相关系数用英文小写r。样本数用英文小写n。概率用英文大写P。     

《病毒学报》来稿需注意的一些常用规范

常用斜体规范:统计学符号:根据国家标准GB3358-82《统计名词及符号》的规定,样本的算术平均数用英文小写斜体x表示,标准差用英文小写斜体s表示,t检验用英文小写斜体t表示,F检验用英文大写斜体F表示,卡方检验用希腊字母小写斜体χ2表示,相关系数用英文小写斜体r表示,自由度用希腊字母小写斜体γ表示,概率用英文大写斜体Ρ表示,样本数用英文小写斜体n表示。     

《中国真菌学杂志》统计学符号著录规范

按GB3358—82《统计学名词及符号》的有关规定书写,常用如下：①样本的算术平均数用英文小写互（中位数仍用M）。②标准差用英文小写s。③标准误用英文小写Si。④t检验用英文小写t。⑤F检验用英文大写F。⑥卡方检验用希文小写x2。⑦相关系数用英文小写r。⑧自由度用希文小写口。⑨概率用英文大写P（P值前应给出具体检验值,如t值、x2值、q值等）。以上符号均用斜体。     

Biochemical Identification of the Two Races of Radopholus similis by Polyacrylamide Gel Electrophoresis

Analysis of proteins of the banana and citrus race of Radopholus similis was carried out by several different types of polyacrylamide gel electrophoresis. These included standard slab gel, SDS slab gel, gradient slab gel, and two-ditnensional slab gel electrophoresis. A major band difference was detected between the two races by slab gel electrophoresis. However, several other poorly resolved but consistent hands of high molecular weight proteins near the gel origin also were considered as diagnostic. Resolution of protein bands was greatly improved by SDS and gradient slab gel electrophoresis, but no differences could be detected among the proteins resolved between the two rares with these techniques. Two-dimensional gels revealed a large number of proteins, but background staining obscured them hindering interpretation. When nematode races were reared on three different host plants, no differences in protein patterns were detected between them, indicating host preferences does not play a role in determining the types proteins occurring in these nematodes.     

Location and purification of enzymes on polyacrylamide gels using dialyzable fluorescent markers

A method for the location of proteins/enzymes by polyacrylamide gel electrophoresis using dialyzable low-molecular-weight fluorescent peptide markers is described. The markers prepared by treating the peptic digest of casein with fluorescamine showed several bands on gel electrophoresis which helped in locating the proteins. The located desired protein could subsequently be purified by extraction.     

Studies on structural proteins of the rat liver ribosomes. I. Molecular wights of the proteins of large and small subunits.

Structural proteins of active 60-S and 40-S subunits of rat liver ribosomes were analysed by two-dimensional polyacrylamide gel electrophoresis. 35 and 29 spots were shown on two-dimensional gel electrophoresis of proteins from large and small subunits, respectively. It was noted that the migration distances of stained proteins with Amido black 10B remained unchanged in the following sodium dodecyl sulfate-acrylamide gel electrophoresis, although some minor degradation and/or aggregation products were observed in the case of several ribosomal proteins, especially of those with high molecular weights. This finding made it possible to measure the molecular weight of each ribosomal protein in the spot on two-dimensional gel electrophoresis by following sodium dodecyl sulfate-acrylamide gel electrophoresis. The molecular weights of the protein components of two liver ribosomal subunits were determined by this 'three-dimensional' polyacrylamide gel electrophoresis. The molecular weights of proteins of 40-S subunits ranged from 10 000 to 38 000 and the number average molecular weight was 23 000. The molecular weights of proteins of 60-S subunits ranged from 10 000 to 60 000 and the number average molecular weight was 23 900.     

Resolution of erythrocyte membrane proteins by two-dimensional electrophoresis.

A two-dimensional electrophoresis method has been developed which solubilizes erythrocyte membrane proteins, and which resolves the components of the band that migrates in detergent gels as if its molecular mass were 95,000 daltons. This method uses gel electrophoresis with sodium dodecyl sulfate in the first dimension and phenol, aqueous urea, and acetic acid in the second dimension. The 95,000 dalton band is known to contain several different membrane proteins, including those associated with anion transport, glucose transport, and (Na+,K+) transport. Two-dimensional electrophoresis resolved this band into one major spot and several minor ones. Pronase digestion of whole erythrocytes, followed by preparation of ghosts and two-dimensional electrophoresis, showed that only the major component of this band was digested by pronase.     

A novel system for the two-dimensional electrophoresis of membrane proteins.

Membrane proteins were resolved in two dimensions by a novel technique that uses discontinuous electrophoresis in both directions. After electrophoresis in the first direction in chloral hydrate, the membrane proteins were further resolved by a novel system that used organic-base dodecyl sulphates to stack and then resolve them. This latter system has several advantages over conventional electrophoresis in sodium dodecyl sulphate, notably that it avoids the production of artifacts generated by other systems.     

Cetyltrimethylammonium bromide discontinuous gel electrophoresis: Mr-based separation of proteins with retention of enzymatic activity.

A discontinuous polyacrylamide and agarose gel electrophoresis system is presented here which allows the fine separation of proteins based on molecular weight with the concomitant retention of native enzymatic activity. This system, referred to as the CAT gel, uses the cationic detergent cetyltrimethylammonium bromide (CTAB) and includes a stacking gel based on the zwitterion arginine and the buffer N-tris(hydroxymethyl)-methylglycine. The CAT gel system allows specific enzyme histochemical detection and localization of proteins after gel electrophoresis. We present evidence that the CAT system stacked and separated a broad range of proteins into discrete bands which migrate as a linear function of log Mr. We have also assessed the effect of CTAB solubilization on the activity of several proteins and showed that some proteins separated by CAT electrophoresis maintain high levels of native enzymatic activity and may be detected histochemically in situ.     

Isoelectric points and molecular weights of salt-extractable ribosomal proteins.

Rat liver ribosomes prepared in low salt buffer contain basic and acidic proteins not found on ribosomes washed in high salt buffer. Proteins extracted from liver ribosomes by 500 mM KCL were characterized by acid urea-polyacrylamide gel electrophoresis, sodium dodecyl sulfate - polyacrylamide gel electrophoresis and gel isoelectric focusing. The salt-solubilized proteins contain 12 polypeptides with a molecular weight over 67000, several polypeptides with molecular weights less than 67 000, and three polypeptides whose molecular weight exceeded 130 000. Ten to 12 of the proteins were basic, and about 24 acidic proteins were partially or wholly extracted from the ribosomes. Four of the acidic proteins have isoelectric points less than 4.5.     

A method for the two-dimensional electrophoresis of leaf proteins

Proteins extracted from green leaves of tobacco were subjected to analysis by two-dimensional electrophoresis. It was found that electrophoretic separations were unsatisfactory when leaf extracts were analyzed directly without prior extraction of pigments, phenols, and lipids by acetone treatment. The plant pigments and several phenolic compounds present in leaves presumably interacted with the proteins and created charge heterogeneity, streaking, and other artifacts. It was found that these problems could be overcome by treatment of leaf extracts with acetone followed by solubilization and electrophoresis of the acetone-treated proteins. Leaf extracts were prepared by grinding deribbed leaf disks in a buffer containing 5 mm potassium carbonate, 9.5 m urea, 0.5 dithiothreitol, 2% Nonidet P-40 detergent, 500 μg/ml l-lysine, and 2% Ampholines. The extracts, after centrifugation to remove cell debris and insoluble material, were treated several times with ice-cold acetone. The acetone-precipitated proteins were treated with nucleases, reprecipitated with cold acetone, and then resuspended in the above grinding buffer. The presence of l-lysine and Ampholines were required for good electrophoretic separations. The resuspended proteins were subjected to two-dimensional electrophoresis and proteins detected by staining and or fluorography. At least 300 distinct proteins could be recognized in radioactive samples. The method gives reproducible patterns even after repeated freezing and thawing of the samples.     

Silver staining of proteins on electroblotting membranes and intensification of silver staining of proteins separated by polyacrylamide gel electrophoresis

A fast and convenient method for silver staining of proteins on electroblotting membranes was developed based on Gallyas' histochemical intensifier and applied to human endothelial cell proteins separated by one- and two-dimensional electrophoresis and electroblotted to polyvinyl difluoride membranes. The method allowed detection of proteins on membranes with a sensitivity equal to the sensitivity of the most sensitive silver-staining protocols for electrophoresis gels. Also, the method was compatible with preceding immunostaining on the same membrane. Furthermore, an intensifying method for proteins in silver-stained SDS-PAGE gels was developed based on Gallyas' histochemical intensifier. This method was applied to proteins separated by one- and two-dimensional gel electrophoresis and visualized by one of several silver-staining methods. Maximal intensification was achieved for the less sensitive but fast acidic silver-staining protocols, but even for the very sensitive alkaline protocols a significant increase in signal to noise ratio was obtained. In particular, negatively stained or invisible proteins on the silver-stained gels were found to be visualized by the Gallyas stain. Proteins from silver-stained and Gallyas-stained gels were identified by mass spectrometry, and the intensification procedure was fully compatible with mass spectrometry.