中国沿海代表性河口地区鳗苗群体形态特征的比较研究

本文报道了１９９２—１９９４年连续３年采自海南至辽宁（包括台湾）沿海７个代表性河口地区鳗苗群体的主要形态特征比较研究结果。４项计数性状和３项度量性状,差异系数分析结果未达到亚种差异水平;判别函数显示,大多数群体间存在显著差异,这种差异应源于遗传变异。各年差异变化无规律,可能与鳗苗漂游分布的随机性有关。     

An abscisic acid analog inhibits abscisic acid-induced freezing tolerance and protein accumulation, but not abscisic acid-induced sucrose uptake in a bromegrass (Bromus inermis Leyss) cell culture

The application of abscisic acid (ABA), either as a racemic mixture or as optically resolved isomers, increases freezing tolerance in a bromegrass (Bromus inermis Leyss) cell culture and induces the accumulation of several heat-stable proteins. Two stereoisomers of an ABA analog, 23 dihydroacetylenic abscisyl alcohol (DHA), were used to study the role of ABA-induced processes in the acquisition of freezing tolerance in these cells. Freezing tolerance was unchanged in the presence of (–) DHA (LT₅₀ -9°C), and no increase in heat-stable protein accumulation was detected; however, the (+) enantiomer increased the freezing tolerance (LT₅₀ -13°C) and induced the accumulation of these polypeptides. All three forms of ABA increased freezing tolerance in the bromegrass cells, although (–) ABA was less effective than either (+) or (±) ABA when added at equal concentrations. Cells pretreated with 20 or 50 M (–) DHA displayed lower levels of freezing tolerance following the addition of 2.5, 7.5 or 25 M (±) ABA. Full freezing tolerance could be restored by increasing the concentration of (±) ABA to > 25 M. Pretreatment of cells with (–) DHA (20 or 50 M) had no effect on freezing tolerance when 25 M (+) ABA was added. The induction of freezing tolerance by 25 M (–) ABA was completely inhibited by the presence of 20 M (–) DHA. The accumulation of ABA-responsive heat-stable proteins was inhibited by pretreatment with 20 M (–) DHA in cells treated with 2.5 or 7.5M (+) ABA, and in cells treated with 25 M (–) ABA. The accumulation of these polypeptides was restored when (±) or (+) ABA was added at a concentration of 25 M. The analysis of proteins which cross-reacted with a dehydrin antibody revealed a similar inhibitory pattern as seen with the other ABA-responsive proteins. The effects of the various isomers of ABA and DHA on cell osmolarity and sucrose uptake was also investigated. In both cases, (±) and (+) ABA had pronounced effects on the parameters measured, whereas (–) ABA treated cells gave substantially different results. In both sucrose uptake and cell osmolarity, DHA had no significant effect on the results obtained following (±) or (+) ABA treatment. Maximum freezing tolerance was only observed in cells when both heat-stable protein accumulation and sucrose uptake were observed.Abbreviations ABA abscisic acid - DHA 2,3 dihydroacetylenicabscisyl alcohols - DMSO dimethyl sulfoxide - LT₅₀ temperature at which 50% of cells are killed The authors would like to acknowledge the technical assistance of Angela Bollman, Bruce Ewan and Angela Shaw. This work was supported by grants from the Natural Science and Engineering Research Council of Canada to L.V.G. and N.H.L., and a grant from the University of Saskatchewan to R.W.W.     

利用激光微束穿刺法将外源基因导入小麦的研究

用激光微束穿刺法将携带有新霉素磷酸转移酶（ＮＰＴ－Ⅱ）基因的质粒ｐＪＩＴ１０１导入京花１号小麦幼胚细胞。方法是将小麦幼胚细胞进行高渗缓冲液预处理,用微米级的激光微束处理,然后在卡那霉素培养基上筛选出具抗性的愈伤组织及绿色小植株。第一年,从１５０个小麦幼胚中,在卡那霉素培养基上筛选出４株绿苗,取两株进行ＮＰＴ－Ⅱ酶活性分析,测到了ＮＰＴ－Ⅱ酶的活性。第二年重复实验,从２４５个小麦幼胚中,经筛选获得１株绿苗,进行了叶片ＤＮＡＰＣＲ扩增检测,转化的绿色小苗扩增出所导入的ＮＰＴ－Ⅱ基因编码的片段。结果表明,外源ＮＰＴ－Ⅱ基因已导入了小麦,并实现了整合表达。     

东北地区生态环境中的Se及其生态效应

对东北地区不同环境要素Ｓｅ的分布与转化规律的研究表明,基岩、土壤、粮食和动物毛Ｓｅ含量分别为０．１２、０．１５０－０．５４０、０．００９６－０．０７６５和０．０４０５－０．１４１４μｇ．ｇ＾－１;城市和农村儿童发Ｓｅ含量为０．４６０和０．１８２μｇ．ｇ＾－１。根据不同要素Ｓｅ含量和生态效应,可将该区分为Ｓｅ适宜区、缺乏区和过渡区３个１级区,每个１级区又分为高Ｓｅ源区的低Ｓｅ源区。     

耐碱性芽孢杆菌碱性淀粉酶的研究：Ⅱ.菌株的诱变与产酶条件

耐碱性巨大芽孢杆菌（Ｂａｃｉｌｌｕｓ ｍｅｇａｔｅｒｉｕｍ）９－Ａ２经紫外线、甲基磺酸乙酯和硫酸二乙酯等多次诱变处理,获得一株产碱性α－淀粉酶能力较高的变异株Ｌ－４９。Ｌ－４９菌株比出发株的产酶能力提高近２．５倍,当以酵母膏为氮源,可溶性淀粉为碳源,初始ｐＨ９￣１０,种龄１８ｈ,接种量５％（Ｖ／Ｖ）,３０℃培养４８ｈ,酶活力可达７３０μ／ｍｌ。     

鳗鱼肌肉的氨基酸及营养价值

通过对优质食用鱼类—鳗鱼肌肉的氨基酸进行测定证实,鳗鱼较之其它鱼类是一种营养价值更高、滋味更鲜美的鱼类。并且,根据结果氨基酸组成比例,可为鳗鱼的人工饲养等方面的研究提供理论依据。     

A gene at 59 minutes on the Escherichia coli chromosome encodes a lipoprotein with unusual amino acid repeat sequences.

We report a 1.432-kb DNA sequence at 59 min on the Escherichia coli chromosome that connects the published sequences of the pcm gene for the isoaspartyl protein methyltransferase and that of the katF or rpoS (katF/rpoS) gene for a sigma factor involved in stationary-phase gene expression. Analysis of the DNA sequence reveals an open reading frame potentially encoding a polypeptide of 379 amino acids. The polypeptide sequence includes a consensus bacterial lipidation sequence present at residues 23 to 26 (Leu-Ala-Gly-Cys), four octapeptide proline- and glutamine-rich repeats of consensus sequence QQPQIQPV, and four heptapeptide threonine- and serine-rich repeats of consensus sequence PTA(S,T)TTE. The deduced amino acid sequence, especially in the C-terminal region, is similar to that of the Haemophilus somnus LppB lipoprotein outer membrane antigen (40% overall sequence identity; 77% identity in last 95 residues). The LppB lipoprotein binds Congo red dye and has been proposed to be a virulence determinant in H. somnus. Utilizing a plasmid construct with the E. coli gene under the control of a phage T7 promoter, we demonstrate the lipidation of this gene product by the incorporation of [3H]palmitic acid into a 42-kDa polypeptide. We also show that treatment of E. coli cells with globomycin, an inhibitor of the lipoprotein signal peptidase, results in the accumulation of a 46-kDa precursor. We thus designate the protein NlpD (new lipoprotein D). E. coli cells overexpressing NlpD bind Congo red dye, suggesting a common function with the H. somnus LppB protein. Disruption of the chromosomal E. coli nlpD gene by insertional mutagenesis results in decreased stationary-phase survival after 7 days.     

DcrA, a c-type heme-containing methyl-accepting protein from Desulfovibrio vulgaris Hildenborough, senses the oxygen concentration or redox potential of the environment.

The amino acid sequence of DcrA from Desulfovibrio vulgaris Hildenborough, a strictly anaerobic, sulfate-reducing bacterium, indicated homology with the methyl-accepting chemotaxis proteins from enteric bacteria (A. Dolla, R. Fu, M. J. Brumlik, and G. Voordouw, J. Bacteriol. 174:1726-1733, 1992). The homology is restricted to the cytoplasmic C-terminal signaling domain. The periplasmic N-terminal sensor domain was found to contain a unique sequence, CHHCH, corresponding to a consensus c-type heme binding site. A pretreated, DcrA-specific polyclonal antiserum, generated against DcrA protein overproduced in Escherichia coli, was used for immunoprecipitation of 35S-labeled DcrA from D. vulgaris and Desulfovibrio desulfuricans G200(pJRFR2), a transconjugant that overexpresses functional DcrA. Labeling of the latter with the heme precursor 5-amino-[4-14C]levulinic acid, followed by immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and fluorography, confirmed the presence of c-type heme, while labeling with L-[methyl-3H]methionine in the absence of protein synthesis confirmed that DcrA is a methyl-accepting protein. The base liability of the incorporated radioactivity indicated methyl ester formation like that occurring in the methyl-accepting chemotaxis proteins of enteric bacteria. L-[methyl-3H]methionine labeling of D. desulfuricans G200(pJRFR2) under different conditions indicated that methyl labeling of DcrA decreased upon addition of oxygen and increased upon subsequent addition of the reducing agent dithionite. These results indicate that DcrA may serve as a sensor of oxygen concentration and/or redox potential.