买麻藤茎的结构及其异常次生生长

买麻藤(Gnetum montanum Mgr.)茎的各类组织的排列与被子植物的茎非常相似,其次生生长也属同一类型。其中最明显的相似之处,是木质部中的导管和韧皮部中的筛分子与“伴胞”。藤本植物买麻藤,正常的次生生长开始后,由每一维管束外侧的薄壁组织经脱分化产生新的形成层,以后逐渐形成一圈维管束。这与前人所描述的新形成层来自韧皮薄壁组织是不同的。异常的维管束与正常的一样,由木质部和韧皮部组成,并被髓射线分隔呈楔形。当第一轮维管束停止生长以后,在其外围以同样方式形成新的一轮,以后并可连续形成多轮。     

羧基化多壁碳纳米管、混合盐及其复合胁迫对水稻幼苗生理特性的影响

将水稻（Oryza sativa L.）幼苗悬浮培养于含有羧基化多壁碳纳米管MWCNTs-COOH（0、2.5、5.0、10.0 mg/L）、50 mmol/L混合盐（1NaCl：9Na₂SO₄：9NaHCO₃：1Na₂CO₃）,以及MWCNTs-COOH+混合盐的复合溶液中,10 d后检测叶片生理生化指标变化,研究MWCNTs-COOH复合盐碱胁迫对水稻幼苗的毒性及生态风险。结果显示,与对照组相比,MWCNTs-COOH单一组诱导下水稻叶片O₂^·-和H₂O₂的产生不明显,而混合盐组和混合盐+MWCNTs-COOH复合组均诱导了O₂^·-和H₂O₂产物的大量累积。MWCNTs-COOH与混合盐复合后,加剧了O₂^·-和H₂O₂的累积,并有明显的浓度效应。活性氧（ROS）作为信号分子在一定程度上诱导了各处理组部分抗氧化酶（SOD、CAT、POD、APX）活性的升高;与混合盐组相比,低浓度混合盐+MWCNTs-COOH复合组中叶绿素a和胡萝卜素含量呈一定程度的升高;MWCNTs-COOH与混合盐复合后,抑制了叶片中可溶性糖（SS）和脯氨酸（Pro）的合成,致使相对电导率（REC）和丙二醛（MDA）含量显著升高。上述抗氧化酶活性及叶绿素a和胡萝卜素含量的升高对缓解水稻叶片氧化损伤、维持正常的光合电子传递及对过剩光能的热耗散是有益的,是水稻幼苗重要的防御机制。本研究表明MWCNTs-COOH单一处理在一定程度上诱导了水稻叶片的氧化胁迫和应激响应,与混合盐复合后加剧了叶片的氧化胁迫和应激损伤。     

小麦根系特征对干旱胁迫的响应

干旱胁迫时, 小麦(Triticum aestivum)根系率先产生应激响应, 同时向地上部发出信号, 诱导地上部发生生理反应, 从而提高植株抗旱能力。根系构型包括平面几何性状和立体几何结构(即拓扑构型), 具有遗传稳定性和可塑性。干旱胁迫影响根系理化特性, 如根源化学信号、根系细胞酶类和根系渗透作用的响应。根系通过调整其解剖学结构和水分吸收动力等来适应干旱胁迫。该文从根系构型、理化特性和解剖学结构3个方面, 系统阐述了小麦根系特征对干旱胁迫的响应, 并探讨了其与干旱胁迫的关系和当前研究中存在的问题, 以期为相关研究提供参考。     

荧光显微镜观察大蒜油对腹水癌细胞的影响

用吖啶橙染色,荧光显微镜观察大蒜油对—S180,昆明小鼠,U14 C57BL/6J小鼠和L1210DBA小鼠的癌细胞作用的影响,结果表明大蒜油有直接破坏癌细胞的DNA,RNA和分裂中期染色体的作用。给药后2—6小时作用最强,12小时后癌细胞数逐渐恢复,因此给药间隔不应超过12小时。我们研究证实大蒜油有明显的抗癌作用,为临床应用提供有力的依据。     

浙北平原水杉人工林生物量的研究

 本文对浙江省北部平原水杉人工林的生物量和生产力进行了测定和研究。按平均标准木法分别调查了干、枝、叶、根的生物量。据调查材料,用相对生长规律建立了估测单株林木各器官干重的回归方程,方程的相关系数和估测精度符合要求,具实用价值。研究结果表明：水杉人工林生物量随年龄的增长而增加,林带18年生后增加速度变缓,片林生物量普遍大于林带生物量,生物量组成比例因年龄而异。随着年龄的增加,年平均净生产量、叶面积指数、光能利用率均逐步加大,至18年生时,上述指标分别为17.51t／ha·a、9.1和0.77%。叶净光合生产率以速生阶段为最大,衰退阶段为最低,当叶净光合生产率急剧下降时,可实施主伐更新。     

由大肠杆菌中提取重组猪生长激素的研究

 本文通过研究提出了一种由大肠杆菌细胞中提取重组猪生长激素的方法。提取回收率为52.4％,纯度为94.1％,具有生物学活性。     

Expression of a gene encoding a rabbit sperm membrane protein in mammalian cells.

A general mammalian expression vector designated pSV2-EP was reconstructed by inserting an oligonucleotide fragment into pSV2-dhfr. This vector allowed insertion of cDNAs with EcoRI cohesive ends. The pSV2-EP contains a simian virus 40 (SV40) early promoter, origin for DNA replication, SV40 poly-A site, splicing site, an initiator ATG downstream from the promoter and an EcoRI site for the insertion of cDNA fragment screened from lambda gt11 expression libraries. A recombinant plasmid (pS-VRS-1) was constructed by inserting RSD-1, a cDNA encoding a rabbit sperm tail protein, into the EcoRI site of the pSV2-EP vector. Chinese hamster ovarian (CHO) dhfr-negative cells were cotransformed with pSV2-dhfr and pSVRS-1 by the calcium phosphate method. In selective culture medium without thymidine and hypoxanthine, several cell lines were obtained containing mRNA and DNA that hybridized with RSD-1. One of these transformed cell lines stained intensely with anti-rSMP-B antibodies, demonstrating that the RSD-1 was expressed in the transformed CHO cells.     

Isolation and characterization of developmentally regulated chondroitin sulfate and chondroitin/keratan sulfate proteoglycans of brain identified with monoclonal antibodies

A panel of monoclonal antibodies prepared to the chondroitin sulfate proteoglycans of rat brain was used for their immunocytochemical localization and isolation of individual proteoglycan species by immunoaffinity chromatography. One of these proteoglycans (designated 1D1) consists of a major component with an average molecular size of 300 kDa in 7-day brain, containing a 245-kDa core glycoprotein and an average of three 22-kDa chondroitin sulfate chains. A 1D1 proteoglycan of approximately 180 kDa with a 150-kDa core glycoprotein is also present at 7 days, and by 2-3 weeks postnatal this becomes the major species, containing a single 32-kDa chondroitin 4-sulfate chain. The concentration of 1D1 decreases during development, from 20% of the total chondroitin sulfate proteoglycan protein (0.1 mg/g brain) at 7 days postnatal to 6% in adult brain. A 45-kDa protein which is recognized by the 8A4 monoclonal antibody to rat chondrosarcoma link protein copurifies with the 1D1 proteoglycan, which aggregates to a significant extent with hyaluronic acid. A chondroitin/keratan sulfate proteoglycan (designated 3H1) with a size of approximately 500 kDa was isolated from rat brain using monoclonal antibodies to the keratan sulfate chains. The core glycoprotein obtained after treatment of the 3H1 proteoglycan with chondroitinase ABC and endo-beta-galactosidase decreases in size from approximately 360 kDa at 7 days to approximately 280 kDa in adult brain. In 7-day brain, the proteoglycan contains three to five 25-kDa chondroitin 4-sulfate chains and three to six 8.4-kDa keratan sulfate chains, whereas the adult brain proteoglycan contains two to four chondroitin 4-sulfate chains and eight to nine keratan sulfate chains, with an average size of 10 kDa. The concentration of 3H1 increases during development from 3% of the total soluble proteoglycan protein at 7 days to 11% in adult brain, and there is a developmental decrease in the branching and/or sulfation of the keratan sulfate chains. A third monoclonal antibody (3F8) was used to isolate a approximately 500-kDa chondroitin sulfate proteoglycan comprising a 400-kDa core glycoprotein and an average of four 28-kDa chondroitin sulfate chains. In the 1D1 and 3F8 proteoglycans of 7-day brain, 20 and 33%, respectively, of the chondroitin sulfate is 6-sulfated, whereas chondroitin 4-sulfate accounts for greater than 96% of the glycosaminoglycan chains in the adult brain proteoglycans.(ABSTRACT TRUNCATED AT 400 WORDS)     

Localization of dystrophin relative to acetylcholine receptor domains in electric tissue and adult and cultured skeletal muscle

Two high-affinity mAbs were prepared against Torpedo dystrophin, an electric organ protein that is closely similar to human dystrophin, the gene product of the Duchenne muscular dystrophy locus. The antibodies were used to localize dystrophin relative to acetylcholine receptors (AChR) in electric organ and in skeletal muscle, and to show identity between Torpedo dystrophin and the previously described 270/300-kD Torpedo postsynaptic protein. Dystrophin was found in both AChR-rich and AChR-poor regions of the innervated face of the electroplaque. Immunogold experiments showed that AChR and dystrophin were closely intermingled in the AChR domains. In contrast, dystrophin appeared to be absent from many or all AChR-rich domains of the rat neuromuscular junction and of AChR clusters in cultured muscle (Xenopus laevis). It was present, however, in the immediately surrounding membrane (deep regions of the junctional folds, membrane domains interdigitating with and surrounding AChR domains within clusters). These results suggest that dystrophin may have a role in organization of AChR in electric tissue. Dystrophin is not, however, an obligatory component of AChR domains in muscle and, at the neuromuscular junction, its roles may be more related to organization of the junctional folds.