大鼠白蛋白mRNA3''''端顺序的分子克隆(简报)

白蛋白与甲胎蛋白基因是由同一祖先基因进化而来。在小鼠,它们是一前一后定位在同一条染色体DNA上。在个体发育和肝癌变过程中,这两基因的相互关系也呈现相反的表达水平。因此,研究甲胎蛋白基因表达的调控与白蛋白基因是不可分割的。本文简要报道我们克隆了大鼠白蛋白mRNA 3′端顺序,为研究白蛋白基因结构和表达提供了必要的探针。白蛋白mRNA是从Wistar大鼠肝脏用双抗体免疫沉淀法提取。分子克隆技术基本是按“分子克隆”实验手册进行。     

亚东璃眼蜱的延迟交配对吸血时间和生殖力的影响

蜱类种群密度的制约因素包括生物的和非生物的两类,分析和认识这些规律,对蜱类的防治上有重要意义。 蜱类的生殖是维持种群密度的重要一环。后肛沟类硬蜱的雌虫当吸附在宿主体时,由于某些原因可发生延迟交配现象。蜱类延迟交配对生育力的影响,在这方面的研究较少。本文为亚东璃眼蜱Hyalomma asiaticum kozlovi Olenev的延迟交配对吸血时间、饱食后的体重以及产卵量等的试验研究结果。     

蛴螬病原菌(Bacillus sp.)的初步研究

蛴螬是农林生产上的重要地下害虫,由于长期栖居地下,防治较为困难。多年实践证明,采用综合防治措施可以有效地控制为害,利用病原微生物防治蛴螬是综合防治中的一个环节,是值得今后深入研究的课题。 1975年9月,我们在河北省任邱县白洋淀附近玉米地采到数头自然患病的阔胸犀金龟(Pento-don patruelis Frivaldszkz)三龄幼虫。1976年5     

精河株斑点热立克次体在非洲钝缘蜱体内的分布

本文报告用乙二醇甲基丙烯酸(GMA)包埋、切片和姬姆萨染色观察精河株斑点热立克次体在非洲钝缘蜱(Ornithodoros moubata)体内的分布情况。接种立克次体后2天,即可从蜱的血淋巴涂片中查见立克次体,但各器官和组织的切片6天后才开始出现阳性,尤以中肠最迟。叮咬感染的蜱的中肠感染较早也较严重。无论接种或叮咬感染,除睾丸和精子外,所查的器官和组织包括涎腺、基节器、中肠、直肠、卵巢以及雄蜱的附腺和贮精囊等切片中都查见立克次体。有的蜱感染很严重,立克次体充满了许多器官和组织的细胞。     

菜粉蝶幼虫感染颗粒体病毒后线粒体形态异常变化的初步观察

病毒侵入昆虫后引起细胞器形态变化的报道很少。我们进行菜粉蝶颗粒体病毒组织病理观察时,在脂肪细胞中,观察到线粒体有异常形态变化现象,现简要报道如下。 用病毒悬液浸湿甘蓝叶,晾干后饲喂3龄幼虫,感染后第3天,截取虫体中段,戍二醛和锇酸固定,618环氧树脂包埋,醋酸铀染色,透射电镜观察。 在脂肪细胞的超薄切片中,可以看到有些线粒体近似环状或液泡状,在有的切片中,此种线粒体的比例很大(图版Ⅰ:2),但在正常幼虫脂肪组织的超薄切片中,极少观察到此种形状的线粒体(图版Ⅰ:1)。     

非洲钝缘蜱传播精河株斑点热立克次体的途径

非洲钝缘蜱(Ornithodoros moubata)叮咬感染精河株斑点热立克次体的豚鼠后45-52天,再叮咬正常豚鼠,可使后者感染。除个别蜱外,受精的感染雌蜱第一次产的卵(吸感染血后10—19天产出)和1龄稚蜱均为阴性。间隔.1个月又喂以正常豚鼠血,这些蜱第二次的吸血率、产卵数和卵的孵化率都明显降低,但从第二次六的卵和1龄稚蚌压印片中均查见大量立克次体。经卵传递率60%,子代感染率59%(6-100%)。     

普劳螨属一新种记述（蜱螨亚纲：巨须螨科）

本文记述普劳螨属一新种:宽颚普劳螨Pulaeus platygnathus sp.nov.,并与近似种马丁普劳螨Pulaeus martini Den Heyer,1981进行了比较。     

Depolymerization of cortical microtubules is not a primary cause of chilling injury in corn (Zea mays L. cv Black Mexican Sweet) suspension culture cells

Cold-induced depolymerization of cortical microtubules were examined in suspension culture cells of corn (Zea mays L. cv Black Mexican Sweet) at various stages of chilling. In an attempt to determine whether microtubule depolymerization contributes to chilling injury, experiments were carried out with and without abscisic acid (ABA) pretreatment, since ABA reduces the severity of chilling injury in these cells. Microtubule depolymerization was detectable after 1 h at 4°C and became more extensive as the chilling was prolonged. There was little chilling injury after 1 d at 4°C in either ABA-treated or non-ABA-treated cells. After 3 d at 4°C, there was about 26% injury for ABA-treated and 40% injury for non-ABA-treated cells, as evaluated by 2,3,5-triphenyl-tetrazolium chloride reduction and by regrowth. After 1d at 4°C, less than 10% of cells retained full arrays of microtubules in both ABA-treated and non-ABA-treated cells, the remainder having either partial arrays or no microtubules. After 3d at 4°C, about 90% of cells showed complete or almost complete depolymerization of microtubules in both ABA-treated and non-ABA-treated cells. ABA did not stabilize the cortical microtubules against cold-induced depolymerization. In about 66% of ABA-treated cells and 57% of non-ABA-treated cells that had been held at 4°C for 3d, repolymerization of cortical microtubules occurred after 3h at 28°C. These results argue against the hypothesis that depolymerization of cortical microtubules is a primary cause of chilling injury.     

High-mobility group and other nonhistone substrates for nuclear histoneN-acetyltransferase

A variety of nonhistone proteins and polyamines has been studied for their substrate activity for nuclear histone N-acetyltransferase. Nonhistone chromatin high-mobility group (HMG) proteins are found to be as good a substrate for the enzyme as histones. The enzyme also acetylates spermidine and spermine. However, protamine, bovine serum albumin, and ubiquitin are not substrates. Chymotryptic peptides of histone and HMGs retained about 64% of the substrate activity, but trypsin treatment reduced the substrate activity by more than 85%. Both N-acetyltransferase activities for HMGs and histones are copurified through salt extraction, polyethylene glycol fractionation, and chromatography on DEAE-cellulose, phosphocellulose columns, and a HPLC anionic-exchange column. The highly purified nuclear histone acetyltransferase shows similar optimal pH and ping-pong kinetics for both HMGs and histones. The Km for HMG is 0.25 mg/ml. HMGs are able to accept the acetyl group from isolated acetyl-enzyme intermediate. Denatured gel analysis shows that HMG 1 and HMG 2 are the major proteins acetylated. High salt concentrations, mononucleotides, and DNA, which inhibit histone substrate activity of the enzyme, also inhibit HMG substrate activity. These observations suggest that there is a major nuclear N-acetyltransferase which is responsible for the acetylation of both histones and HMGs and perhaps also of spermine and spermidine. Thus the regulation of the structure and function of chromatin through postsynthetic acetylation can be achieved by a single nuclear N-acetyltransferase.