医蛭唾液腺分泌物:成分、功能及应用前景

本文对医蛭唾液腺分泌物中主要活性物质的认识发现过程、结构与功能以及医学应用的实例和前景作了扼要的综述。     

害虫,天敌和食料的数学模型

本文从实际问题出发,结合已有的描述群落生态的数学模型,提出了一组描述马尾松毛虫(Dendrolimus pnnctalus,walker)、条毒蛾(Lymantria dissoluta,Swinhoe)、天敌和食料之间动态关系的数学模型: w(k+1=(a_1x(k+1)/(1+a_2x(k+1)/_z(k))+a_3w(k)/(1+a_4w(k)/y(k)) x(k+1)=b_1w(k)/(1+b_2w(k)/y(k))+b_3x(k)/(1+b_4x(k)/z(k))+ y(k+1)=c_1z(k)/[1+c_sz(k)+c_3y(k)][1+c_4w(k)+(k+1)] z(k+1)=d_1z(k)/[1+d_2z(k)][1+d_3x(k)+d_4w(k)] 对于这个模型的线性化形式,详细讨论了控制松毛虫的暴发所需的条件及其生态学机制。     

脲酶抑制剂氢醌的环境效应评价

本文根据用标记和非标记氢醌进行的模拟、盆栽和田间定位试验,结合国内外文献有关氢醌的环境常数,论述了氢醌在土壤-植物系统的去向和代谢途径、对土壤酶活性的影响及其环境效应。得出的结论是:作为脲酶抑制剂使用的微量氢醌(0.3—0.4％,与尿素重量比),不会从土壤中淋失和挥发,在土壤和植物中没有累积,对与碳、氮和磷转化有关的土壤酶活性很少影响。在土壤中,它将通过氧化、臭氧化和生物学降解,经由环断裂生成二元酸或参与腐殖物质的合成。在植物体内,主要通过糖苷化得到同化和利用。因此,氢醌作为脲酶抑制剂在农业生产中应用是安全的。     

组织型纤溶酶原激活剂的发光分析法及其应用

 本文建立了组织型纤溶酶原激活剂(t-PA)活力的发光固相测定方法。用氨基乙基丁基异鲁米诺(ABEI)标记纤维蛋白原(Fg),在一定条件下,t-PA作用于固相(包被ABEI-Fg),产生纤维蛋白的降解产物。测定可溶性降解产物的发光强度,即能计算t-PA活性。该方法的标准曲线范围对t-PA为0.156IU/mL～40IU/mL。灵敏度可达0.156IU/mL。回收率为98.6％(n=27)。批内批间变异系数分别为6.6％及10.3％。该方法曾用于检测细胞培养液中提取t-PA样品及t-PA基因表达时培养液中t-PA的活性。也曾用于检测从组织中纯化t-PA样品及血浆中t-PA活性的测定。文中讨论了该方法与其它方法优缺点的比较。     

~3H-TdR放射线转化C3H/10T1/2细胞株转化生长因子α的研究

本文通过斑点印渍杂交技术和放射免疫分析方法,首次证实,~3H-TdR放射线转化C3H/10T1/2细胞株可高表达TGFα mRNA,并可向细胞外分泌具有免疫活性的TGFα分子,而非转化对应细胞中虽有TG FαmRNA的弱表达,但其无血清培养上清中未测到TGFα的分泌。表明TGFα参与了放射线对细胞的转化以及维持转化细胞增殖的过程。提示TGFα在三大致癌因素转化细胞中的存在可能具有普遍意义。同时,c-myc与c-fos两种癌基因mRNA在转化细胞中的表达水平显著高于非转化对应细胞,而c-sis癌基因mRNA的表达水平在两种细胞中无显著差异。     

Inhibition of rat tissue kallikrein gene family members by rat kallikrein-binding protein and alpha 1-proteinase inhibitor.

The regulation of tissue kallikrein activity by plasma serine proteinase inhibitors (serpins) was investigated by measuring the association rate constants of six tissue-kallikrein family members isolated from the rat submandibular gland, with rat kallikrein-binding protein (rKBP) and alpha 1-proteinase inhibitor (alpha 1-PI). Both these serpins inhibited kallikreins rK2, rK7, rK8, rK9 and rK10 with association rate constants in the 10(3)-10(4) M-1.s-1 range, whereas only 'true' tissue kallikrein rK1 was not susceptible to alpha 1-PI. This results in slow inhibition of rK1 by plasma serpins, which could explain why this kallikrein is the only member of the gene family identified so far that induces a transient decrease in blood pressure when injected in minute amounts into the circulation.     

Ouabain-resistant transfectants of the murine ouabain resistance gene contain mutations in the alpha-subunit of the Na,K-ATPase.

A 6.5-kilobase murine genomic DNA fragment isolated by Levenson et al. (Levenson, R., Racaniello, V., Albritton, L., and Housman, D. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 1489-1493) (called the ouabain resistance gene) has been shown to produce ouabain resistance in primate cells. Preliminary sequence information has revealed no homology with the coding sequence of the Na,K-ATPase. We have introduced this murine sequence into monkey and murine cells in an attempt to characterize its mechanism of action. In our experiments, transfection of this DNA fragment is associated with the low frequency (1 in 8 x 10(5) cells) appearance of ouabain-resistant clones of CV1, COS, and NIH 3T3 cells, an event not seen in control transfections. Characterization of a new clone of ouabain-resistant CV1 cells (called OR8 cells) revealed a 5-fold increase in the IC50 for ouabain inhibition of rubidium uptake and a 10-fold increase in cell survival on ouabain. Although the murine sequence was detectable in Southern blots of ouabain-resistant cells soon after transfection, this exogenous DNA was rapidly lost despite continued exposure to ouabain. Furthermore, we were unable to detect message expression by this genomic sequence in any of the three cell types tested. Instead, we found that all three ouabain-resistant cell lines exhibited point mutations in a domain of the alpha-subunit that has been implicated in ouabain sensitivity (H1-H2). One of these mutations (Asp121-Asn121 in OR8 cells) has been previously reported to cause ouabain resistance (Price, E.M., Rice, D.A., and Lingrel, J.B. (1989) J. Biol. Chem. 264, 21902-21906). Other novel mutations in the H2 transmembrane domain were also detected. We postulate that the "ouabain resistance gene" is important in the early selection process on ouabain but that the permanent ouabain-resistant phenotype is due to a stable mutation in one allele of the alpha-subunit of the Na,K-ATPase.     

Cys residues of the hepatitis B virus capsid protein are not essential for the assembly of viral core particles but can influence their stability.

In the spherical capsid of hepatitis B virus (HBV), intermolecular disulfide bonds cross-link the approximately 180 p21.5 capsid protein subunits into a stable lattice. In this study, we used mutant capsid proteins to investigate the role that disulfide bonds and the four p21.5 Cys residues (positions 48, 61, 107, and 185) play in capsid assembly and/or stabilization. p21.5 Cys residues were either replaced by Ala or removed (Cys-185) by carboxyl-terminal truncation, creating Cys-minus mutants which were expressed in Xenopus oocytes via microinjected synthetic mRNAs. Fractionation of radiolabeled oocyte extracts on 10 to 60% sucrose gradients revealed that Cys-minus core proteins resolved into the nonparticulate and capsid forms seen for wild-type p21.5. On 5 to 30% sucrose gradients, nonparticulate Cys-minus core proteins sedimented as dimers of approximately 40 kDa. We conclude that Cys residues and disulfides are not required for the assembly of either HBV capsids or the dimers that provide the precursors for capsid assembly. Since assembly presumably demands an appropriate p21.5 tertiary structure, it is unlikely that Cys residues are required for proper p21.5 folding. However, Cys residues stabilize isolated p21.5 structures, as evidenced by the marked reduction in stability of Cys-minus dimers and capsids (i) in nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis and (ii) upon protease digestion. We discuss these results in the context of the HBV life cycle and the role of Cys residues in other proteins.