3种发根农杆菌A4转化系毛根的细胞学观察及同工酶酶谱分析

利用根尖压片法对可再生型发根农杆菌A4转化系毛根和不可再生型转化系毛根进行了染色体计数,并利用聚丙稀酰胺凝胶电泳法对其进行过氧化物酶(POD)、细胞色素氧化酶(COD)、酯酶(EST)的同工酶酶谱分析。结果表明：(1)染色体丢失现象在转化的毛根根尖中是普遍存在的,不可再生转化系与可再生转化系相比,染色体丢失比例显著增多;(2)不可再生转化系的POD和COD同工酶酶谱变化较可再生转化系的变化大,且EST含量明显低于可再生转化系。     

紫色甘薯品系6种酶的同工酶分析

采用聚丙烯酰胺凝胶电泳技术,选用过氧化物酶(POD)、超氧化物歧化酶(SOD)、细胞色素氧化酶(CYT)、淀粉酶(AMY)、酯酶(EST)、苹果酸脱氢酶(MDH)等六种酶的同工酶系统对14个紫色甘薯品种(系)进行了同工酶分析.结果表明:过氧化物酶(POD)、细胞色素氧化酶(CYT) 、超氧化物歧化酶(SOD)等三种酶的同工酶酶谱很丰富,分别有13、11、10条酶带;淀粉酶(AMY)、酯酶(EST)、苹果酸脱氢酶(MDH)等三种酶的同工酶酶带相对较少,分别为4、7、7条.聚类分析结果表明,所有供试紫色甘薯品系或品种分成7类:I类包括品系A1、A2、A7;II类包括品系B1～B3;III类包括品系B7和B8;IV类只有品系B9;V类包括品系A3、A4、A6;VI类只有品系A5;VII类只有品种"山川紫".     

金秋梨和新高梨的分子遗传学对比分析

金秋梨和新高梨的形态性状、生物学性状以及酯酶同工酶、过氧化物酶同工酶、细胞色素氧化酶同工酶酶谱均产生了变化。利用异源DNA探针—小麦rDNA克隆pTA71,与四种核酸内切酶PstⅠ、BamHⅠ、EcoRⅠ及BglⅡ酶切消化的金秋梨和新高梨叶片总DNA杂交,结果表明,pTA71-PstⅠ和pTA71-BamHⅠ二种探针—酶组合可在金秋梨和新高梨中检测到RFLP差异。     

小冰麦异附加系列II的同工酶鉴定1)

以普通小麦为遗传背景，分别附加了天蓝冰草1个染色体组中的1条染色体的7个异附加系为材料，采用薄层聚丙烯酰胺凝胶等电聚焦电泳技术，对各异附加系进行了酯酶、过氧化物酶和乙醇脱氢酶的同工酶酶谱带分析，找到了5个异附加系的特征谱带。通过异附加系间的酶谱带差异比较，可将所有异附加系鉴别出来。为今后鉴别异附加系提供了一个快速、简便的方法。     

小冰麦异附加系列II的同工酶鉴定

以普通小麦为遗传背景,分别附加了天蓝冰草1个染色体组中的1条染色体的7个异附加系为材料,采用薄层聚丙烯酰胺凝胶等电聚焦电泳技术,对各异附加系进行了酯酶、过氧化物酶和乙醇脱氢酶的同工酶酶谱带分析,找到了5个异附加系的特征谱带。通过异附加系间的酶谱带差异比较,可将所有异附加系鉴别出来。为今后鉴别异附加系提供了一个快速、简便的方法。     

苜蓿胚状体的分离及其发育过程中三种同工酶酶谱分析(简报)

目前,对胚状体发生过程中的生理生化研究表明,这一过程伴随有核酸、蛋白质等大分子物质合成速度的增加及与胚胎发生有关的特异性蛋白的合成;一些同工酶,如过氧化物酶、脂酶、细胞色素氧化酶和谷氨酸脱氢酶     

禺毛茛复合体及其近缘种过氧化物酶同工酶研究

对国产禺毛茛（RanunculuscantoniensisDC．）复合体及其近缘种8个种的15个居群52个个体的根进行了过氧化物酶同工酶研究,结果表明：①居群内过氧化物酶谱略有变异。同工酶酶谱或多或少能显示居群特征。供试的8个种中没有任何2个种的酶谱完全一致,这说明在种级水平酶谱呈现出高度的分化现象。②根据染色体、孢粉和过氧化酶同工酶的资料推测,除R．silerifolius（2x）外,R．cantoniensis（4x）还有1个亲本。该亲本应具有“短m-型”染色体组,散沟和波状覆盖层的花粉,在其根的过氧化物酶酶谱中至少含A1、A2、C4和C64条酶带。③来自形态、染色体孢粉及同工酶的证据均证实R．vaginatus（5x）可能起源于（R,diffusus（4x）×R．sieboldii（6x）的杂交后代。     

谷子耐盐系的几种同工酶的变化及外源ABA对它们的影响

对谷子细胞变异系的过氧化物酶,细胞色素氧化酶和脂酶同工酶的分析表明：耐盐系在无盐胁迫条件下过氧化物酶同工酶的总酶活性高于对照系,其各同工酶带的强度也与对照有明显差异;在ＮａＣｌ迫条件焉耐盐系中个别原有的酶带消失。细胞色素氧化活性与过氧化物酶同工酶的活性变化情况类似,均与对照有明显差异。     

用5种同工酶分析云南芋种质资源的遗传多样性

用5种同工酶(酯酶、过氧化物酶、超氧化物歧化酶、多酚氧化酶、细胞色素氧化酶)分析云南48份芋材料遗传多样性,并将5种同工酶的酶带检测结果进行聚类分析.结果表明:48份材料的5种同工酶的酶带数分别在11～19条之间,除超氧化物歧化酶仅有3种酶谱类型外,其余4种同工酶的酶谱数均超过检测试材的半数.将聚类结果与试材的植物学性状相比较,发现以来源、用途、生态位和叶柄、叶心颜色等能对聚类结果进行初步分类,并给予合理解释.因此从试材的植物学性状观察、野生和半野生种的存在以及蛋白质表达水平的同工酶分析结果来看,云南省的芋种质资源呈现丰富的遗传多样性.这为芋遗传变异的进一步深入研究以及对正面临巨大威胁的云南芋资源进行原生境保存的可能性提供了依据.     

红豆杉组织培养中SINENXANS高产细胞系Ts19的几种同工酶动态比？…

对从中国红豆杉的茎来源的愈伤组织经筛选而得的ｓｉｎｅｎｘａｎｓ高产细胞系Ｔｓ１９的过氧化物酶（ＰＯＤ）、酯酶（ＥＳＴ）、细胞色素氧化酶（ＣＯＤ）、淀粉酶（ＡＭＬ）、多酚氧化酶（ＰＰＯ）及超氧化物歧化酶（ＳＯＤ）的同工酶,可溶性蛋白的含量及电泳谱带、超氧化物歧化酶、多酚氧化酶和苯丙氨酸解氨酶（ＰＡＬ）的活性作了比较研究。并与培养过程中ｓｉｎｅｎｘａｎｓ含量的动态变化相比较,探索了这几种同工酶的酶谱和     

不同波长的激光对水稻胚芽中可溶性蛋白质及同工酶的作用

用波长0.3371、0.6328μm和1.06μm的激光器,用不同剂量(5、15、50min和3、7、9个脉冲),照射水稻干胚,使其萌动生长72hr后,再用聚丙烯酰胺凝胶电泳法,分析胚芽中可溶性蛋白质,酯酶同工酶和过氧化物酶同工酶。结果证明,波长0.3371～1.06μm的激光辐照水稻种胚,都能使同一生物大分子的活性和分子结构产生变异。由此认为,不能用辐照离体制备液所得结果去预言在活体上的反应。     

家蝇幼虫同工酶研究

本通过聚丙烯酰凝胶电泳法对家蝇幼虫体内的过氧化物酶、乳酸脱氢酶、苹果酸脱氢酶、酯酶和超氧化物歧化酶,以及对超氧化物歧化酶的特性进行了研究。实验结果为家蝇幼虫资源开发利用提供了理论依据。     

DMSO浸种对水稻种子愈伤组织诱导、再分化的影响

用0.2%、1%、5%二甲亚砜(DMSO)浸种处理水稻种子1、3、6小时,可促进种子成熟胚的愈伤组织诱导率,尤以0.2%DMSO浸种1小时效果最好。同时,DMSO浸种还明显促进所诱导的愈伤组织的根、芽分化,其中根分化率以5%DMSO浸种1小时的为最高,而芽分化率以1%DMSO浸种3小时的为最高,表明DMSO对愈伤组织分化芽和分化根的适宜浓度是不同的。DMSO浸种还明显影响细胞透性、过氧化物酶同工酶谱的变化和增强淀粉酶的活性。比较过氧化物酶同工酶酶带3/7及4/10的峰高比值和愈伤组织芽分化率的关系,两者呈正相关。另外,愈伤组织的细胞透性也与芽分化率和总培养效率之间呈正相关。     

CXCR4的抑制性多肽对乳腺癌细胞CXCR4和HER-2表达及HERCEPTIN药物敏感性的影响

目的 探讨CXCR4抑制性多肽对人乳腺癌细胞株SKBR3膜受体HER-2和CXCR4的蛋白表达及其对Herceptin药物敏感性的影响.方法 抑制性多肽、Herceptin单独或联合处理乳腺癌SKBR3细胞24、48h后,用MTT法观测SKBR3细胞的增殖抑制效应;Weatern blot和免疫纽化法检测SKBR3细胞中CXCR4和HER-2蛋白表达;RT-PCR检测HER-2、CXCR4 mRNA的表达,流式细胞仪检测细胞周期的变化.结果 多肽和Herceptin可不同程度地下调人乳腺癌细胞SKBR3中CXCR4和HER-2的蛋白表达.多肽对细胞生长抑制不明显,与Herceptin联合用药后,生长抑制率高于对照组和Herceptin单独用药组(P<0.001),48h生长抑制率为57.94%±5.3,且呈时问依赖(P<0.05),Herceptin单独作用SKBR3-细胞,细胞周期阻滞于G0/GI期,并且S期的比例减少,与多肽联合作用后,细胞周期又进一步阻滞于G2/M期,S期细胞进一步降低.结论 抑制性多肽能不同程度地下调膜受体HER-2和CXCR4的表达,提高人乳腺癌细胞株SKBR3对Herceptin药物的敏感性.     

瘿螨总科科间亲缘关系的初步研究

以聚丙烯酰胺凝胶电泳,测定了瘿螨总科中分属3个科的5种瘿螨的酯酶同工酶,根据电泳谱带和所测5种瘿螨的形态特征,计算出欧氏距离和相似系数,绘制谱系图,表明它们的亲缘关系顺序为:桧三毛瘿螨,金钱松博氏瘿螨,雪柳顶冠瘿螨,女贞刺瘿螨和金银木大嘴瘿螨。其中以雪柳顶冠瘿螨和女贞刺瘿螨的亲缘关系最近,桧三毛瘿螨和金钱松博氏瘿螨亦属较近缘的两个种,金银木大嘴瘿螨则独立于外。这种亲缘关系,构成了纳氏瘿螨科→瘿螨科→大嘴瘿螨科的科间进化关系。     

团头鲂的胚胎及成体组织中八种同工酶系统的研究

用垂直的淀粉凝胶电泳方法分析了胚胎发育阶段(0—105小时)和成体6种组织中的乳酸脱氢酶(LDH)、苹果酸脱氢酶(MDH)、谷氨酸脱氢酶(GDH)、葡萄糖—6—磷酸脱氢酶(G6PD)、醇脱氢酶(ADH)、异柠檬酸脱氢酶(IDH)、酯酶(EST)和碱性磷酸酶(AKP)等8种同工酶系统的酶带。共约有23个基因座位在其胚胎发育期和成体组织中表达。所分析的大多数同工酶在团头鲂个体发生过程中表达的情况大致可分为3种类型：①胚胎发育期间持续存在的同工酶类,它们在成体组织中无特异性分布;②到胚胎发育后期才开始表达的同工酶类,它们往往和特定的组织或器官的形态发生或机能分化紧密相关,并在成体组织中呈特异性分布;③在成体组织中都没有被发现而只在胚胎发育期所特有的同工酶。团头鲂的MDH同工酶类之间以及它们和G6PD同工酶活性变化之间存在着相关性,二者可能存在共同的调控机制。与许多其他鱼类不同,团头鲂的GDH同工酶在整个胚胎发育过程中都有活性,但在其成体组织中无特异性分布。基因调控系统的时空精确性是保证团头鲂胚胎发育正常代谢活动的必要条件。     

吡效隆对花生光合作用及产量的影响

花生结荚期施用０．１～１０ｍｇ／Ｌ吡效隆（４ＰＵ３０）溶液，能增加叶片的厚度，提高叶片叶绿素含量和光合速率，促使叶片中的同化物向荚果运输和积累增多，从而促进了荚果生长和发育，使结荚率、饱果率以及百果重和百仁重增加，最终使单株荚果产量增产１２６％左右，吡效隆的最适浓度为１ｍｇ／Ｌ。     

INDEPENDENT HIGH-FREQUENCY OSCILLATIONS IN THE AMOUNTS OF INDIVIDUAL ISOZYMES OF LACTATE DEHYDROGENASE IN HL60 CELLS

Early studies, using kinetic methods, suggested that the isozyme pattern of lactate dehydrogenase in various cells oscillated with time. More recent electrophoretic studies on murine erythroleukaemic cells (which exhibit only one isozyme) indicated very high frequency variations (period 2min or less) in the amount of the lone active isozyme. We now show that in HL60 cells, the activity stain intensities of the two major isozyme bands both oscillate but the temporal variations are distinct. As with other cellular rhythms, each of the two periodicities seem to be modulated in cyclic fashion with respect to period, amplitude and mean levels, the periods of both the primary and modulating rhythms being of the order of 10–15min or probably much less.     

4PU对萝卜离体子叶衰老的影响

萝卜（Ｒａｐｈａｎｕｓｓａｔｉｖｕｓ）离体子叶在暗中培养过程中,作为叶片衰老指标的叶绿素和蛋白质含量随着培养时间的延长而呈现出稳定的下降。４ＰＵ处理可减轻叶绿素和蛋白质含量的下降,表现出明显的延缓衰老的效应,其中以１０１ｍｇ／Ｌ效果最佳     

Mouse aldehyde dehydrogenase genetics: Positioning of Ahd-1 on chromosome 4

Electrophoretic variants of mitochondrial aldehyde dehydrogenase (AHD-A₂) are widely distributed among inbred strains of Mus musculus and have been used to localize the gene encoding AHD-A₂(Ahd-1) at the non-centromeric end of chromosome 4. In the mouse (Mus musculus), aldehyde dehydrogenase (AHD; E.C.1.2.1.3) exists as at least three isozymes which are differentially distributed in liver subcellular fractions (designated A₂, B₄ and Cy* for the mitochondrial, soluble and microsomal isozymes respectively) and in various tissues of this animal (Holmes, 1978a; 1978b; Timms & Holmes, 1981). Electrophoretic variants have been previously reported for the A₂ and B₄ isozymes among inbred strains of mice, and the genetic loci (designated Ahd-1 and Ahd-2) have been localized on chromosomes 4 and 19 respectively (Holmes, 1978b; Timms & Holmes, 1980). This paper describes further genetic analyses of AHD-A₂ enabling Ahd-1 to be positioned at the non-centromeric end of chromosome 4. Forty-three inbred strains of Mus musculus were used in these studies (Table 1). Two series of matings were carried out. 1) Female SM/J mice and male NZC/B1 mice were mated to obtain F, female offspring which were backcrossed to male NZC/B1 mice. These progeny were used to examine the segregation and linkage relationship of b (brown), Pgm-2 (encoding phosphoglucomutase B) and Ahd-1 (Table 2). 2) Female C57BL/6J mice and male SM/J. mice were mated to obtain F, female offspring which were backcrossed to male SM/J mice. The segregation and linkage relationship of Pgm-2, Gpd-1 (encoding the liver and kidney isozyme of hexose-6 phosphate dehydrogenase) and Ahd-1 were examined for these backcross progeny (Table 3). Methods for preparing liver and kidney extracts and the cellulose acetate electrophoresis procedure for typing Ahd-1, Pgm-2 and Gpd-1 have been previously described (Holmes, 1978b). A previous study has described the electrophoretic patterns for allelic variants for mitochondria1 AHD and of the hybrid phenotype for this enzyme (Holmes, 1978b). The three-allelic isozyme pattern for hybrid animals was consistent with a dimeric subunit structure: AHD-A¹A², AHD-A¹A² and AHD-3, with the A1 and A2 subunits being encoded by separate alleles at a single locus, designated Ahd-1 (Ahd-1^oand Ahd-1^brespectively). The distribution of these alleles among 43 inbred strains of mice is given in Table 1. The allelic variants were approximately equally distributed among the inbred strains examined and no divergence of phenotype was observed among the 6 substrains of C57BL mice (Ahd-1^aallele) and 5 substrains of BALB/c (Ahd-1^ballele) mice examined. Genetic variants for phosphoglucomutase-B (PGM-B) have been reported by Shows, Ruddle and Roderick (1969) and the gene (Pgm-2) was subsequently localized on chromosome 4 near b (brown) by Chapman, Ruddle and Roderick (1970). Table 2 illustrates the results of a three-point cross between b, Pgm-2 and Ahd-1. Variation from the expected 1:1:1:1:1:1 ratio for unlinked loci was significant(x²= 73.15; 7 df; P < 1 × 10^-5), indicating that the three loci are linked. Recombination frequency data are consistent with the gene order: b - Pgm-2 - Ahd-1 The second cross examined the segregation of Pgm-2, Ahd-1 and Gpd-1 loci (Table 3). The latter locus has been previously positioned on chromosome 4 (linkage group VIII) by Hutton & Roderick (1970) and Chapman (1975), and has been used to localize Ahd-1 in this region (Ahd-1 and Gpd-1 exhibit a recombination frequency of 10.3 ± 3.7 %) (Holmes, 1978b). The data from Table 3 is consistent with a gene order of Pgm-2 - Ahd-1 - Gpd-1. The recombination frequency data of Ahd-1 with Gpd-1, Pgm-2 and b also supports the proposal that Ahd-1 is localized between Pgm-2 and Gpd-1 (Tables 2 and 3; Holmes, 1978b). Recent metabolic studies have indicated that mitochondria1 aldehyde dehydrogenase (AHD) plays a very important role in the metabolism of acetaldehyde derived from ethanol, ensuring a low concentration of acetaldehyde in the blood leaving the liver (Grunnet, 1973; Parilla et al., 1974; Corral1 et al., 1976). Moreover, genetic variation of this isozyme in human livers has been recently reported (Harada et al., 1978), and this polymorphism has been proposed as the molecular basis for individual and racial differences in alcohol sensitivity (Goedde et al., 1979). Consequently, genetic analyses of mitochondria1 AHD are of particular significance to studies on the genetic control of alcohol metabolism in mammals. In summary, this report confirms previous studies which demonstrated that the genetic locus encoding mitochondrial aldehyde dehydrogenase in the mouse (Ahd-1) is on chromosome 4 (Holmes, 1978b), and positions the gene with respect to b (brown), Pgrn-2 (encoding phosphoglucomutase B) and Gpd-1 (encoding the liver and kidney isozyme of hexose-6-phosphate dehydrogenase). In addition, the distribution of the 2-allelic phenotypes for this isozyme has been examined among 43 in- bred strains of mice.