两个苜蓿品种营养器官解剖结构特征比较

为了明确具有极强抗虫特性的‘草原4号紫花苜蓿’(Medicago sativa L.‘Caoyuan No.4’) 营养器官的解剖特征,该研究选择具有抗蓟马特性较强的‘草原2号杂花苜蓿’(Medicago varia Martin.‘Caoyuan No.2’)为对照,采用显微镜观察比较两品种的根、茎、叶解剖结构特征,为揭示‘草原4号紫花苜蓿’ 抗蓟马特性提供理论依据。结果显示：(1)‘草原4号紫花苜蓿’根部解剖结构的皮层薄壁细胞厚度、内皮层厚度、形成层厚度、木质部厚度和木射线宽度等5个指标均极显著高于(P＜0.01)‘草原2号杂花苜蓿’,其中木射线宽度(159.37 μm)是‘草原2号杂花苜蓿’的1.82倍。(2)‘草原4号紫花苜蓿’的茎部厚角组织厚度(21.4 μm)极显著高于‘草原2号杂花苜蓿’(P＜0.01),而韧皮部宽度、髓直径却均极显著低于‘草原2号杂花苜蓿’(P＜0.01)。(3)‘草原4号紫花苜蓿’叶片解剖构造的7个指标均极显著高于‘草原2号杂花苜蓿’(P＜0.01),其中栅栏组织层数(2～3层)极明显地高于‘草原2号杂花苜蓿’(1~2层)。研究表明,‘草原4号紫花苜蓿’的组织结构特征具有明显的抗虫特征,且其组织的抗虫特征比‘草原2号杂花苜蓿’更为突出。     

The mobility of chromatophore membranes from Ectothiorhodospira Shaposhnikovii revealed by Rayleigh scattering of Mössbauer radiation (RSMR) experiments

Chromatophores from Ectothiorhodospira Shaposhnikovii in solvents of different viscosity were investigated by RSMR experiments in the temperature range between 112 K and room temperature. Additional RSMR-experiments were done on solvents only. The mobility of the molecules and within the molecules is the given by the Debye-Waller factor which yields the meansquare displacement, , averaged over the atoms in the system. The mobility of the atoms of the chromatophores roughly follows the mobility of the atoms of the solvents. At low temperatures the mobility of the chromatophores remains slightly larger than the mobility of the frozen solvent. At room temperature, however, of the chromatophores remains significantly smaller.Chromatophores in a glycerol-water mixture (0.001 M Tris-HCl buffer) and in water (0.05 M Tris-HCl buffer) show a different dynamic behaviour. A region with enhanced mobility near T=180 K was indicated for the chromatophores in the glycerolwater mixture.A correlation has been suggested between the rate of electron transfer from the primary to the secondary quinone and the increase of the conformational mobility of the chromatophores in glycerol-water mixture.Abbreviations Mb Myoglobin - Met-Mb Metmyoglobin     

Hemoglobin dynamics in rat erythrocytes investigated by Mössbauer spectroscopy

Rats have been enriched in ⁵⁷Fe and erythrocytes were isolated from the blood. Mössbauer absorption spectroscopy on the hemoglobin of these erythrocytes has shown rather similar dynamics as found earlier in crystals of myoglobin, in frozen solutions of human hemoglobin and in a number of other proteins. The results strongly indicate that the motion of the heme and presumably some part of the F-helix is mainly influenced by the average viscosity of the sample determined by a network of hydrogen bridges and other weak interactions. Extrapolations of Mossbauer results from protein crystals to proteins in their physiological surroundings seem to be suitable for heme proteins. Offprint requests to: F. G. Parak     

Assembly of the sarcoplasmic reticulum proteins in differentiating rat skeletal muscle cell cultures: localization by immunofluorescence of sarcoplasmic reticulum proteins in differentiating rat skeletal muscle cell cultures

Immunofluorescent staining techniques were used to study the distribution of the Ca(2) + Mg(2+)-dependent ATPase and calsequestrin in primary cultures of differentiating rat skeletal muscle cells, grown for different periods of time under various culture conditions. In mononucleated myoblasts calsequestrin was detected after 45 h in culture whereas the ATPase was not detected until 60 h. After cell fusion began, both proteins could be identified in all multinucleated cells. Myoblasts grown for longer than 60 h in low Ca(2+) medium contained calsequestrin and the ATPase, even though they were unable to fuse. These studies at the cellular level confirm biochemical findings on the biosynthesis of calsequestrin and the ATPase. Immunofluorescent staining of myoblasts showed that calsequestrin first appears in a well-defined region of the cell near one end of the nucleus. At later times, the staining occupied progressively larger regions adjacent to the nucleus and took on a fibrous appearance. This suggests that calsequestrin first accumulates in the Golgi region and then gradually spreads throughout the cell. In contrast, the ATPase appeared to be concentrated in many small patches or foci throughout the cytoplasm and was never confined to one particular region, although some parts of the cell often stained more intensely than others. In multinucleated cells, alternating dark and fluorescent strands parallel to the longitudinal axis of the cells were evident.     

The use of thermally activated tritium atoms for structural-biological investigations: the topography of the TMV protein-accessible surface of the virus

Thermally activated tritium atoms were used for studying the topography of the TMV protein-accessible surface of the virus. The accessibility profile of amino acid residues in a protein polypeptide chain was determined from data on the intramolecular distribution of a tritium label in the TMV protein. It was shown that tryptic peptides T3, T4, T12, the N-terminal region of peptide T1 and the proximal tryptic peptide T8 (located 20 to 25 A (1 A = 0.1 nm) from the viral axis) are accessible to tritium labelling. The fact of tritiation of the viral RNA was detected as well. This evidence was compared with the high-resolution X-ray analysis data for the TMV. A model is suggested to explain the exposure of the buried sites of the virus to thermally activated tritium atoms. The possibilities and limitations of this method in studying the surface topography of proteins in supramolecular systems as well as for location of protein antigenic regions are discussed.