玉米花粉单倍体植株染色体上异染色质的变异

我们用Giemsa BSG C-带技术检查了玉米花药培养获得的花粉单倍体植株根尖细胞染色体上异染色质的变异,观察结果表明,有的植株所显示的C-带数目是与供体植株的相一致,有的植株所显示的C-带数目则发生了显著变化,其中有的增加,有的减少。并讨论了异染色质发生变异的可能原因。还相应地观察到间期核中染色中心的变化是与中期染色体上C-带数目的变化相一致。     

点叶绵枣叶片培养及器官分化的研究

点叶绵枣叶外植体培养于MS 6-BA 1 PPm IBA 0.5 ppm培养基中,一月后不定芽仅从近轴面的叶表面产生。组织学的观察表明,不定芽起源于表皮细胞。     

南京地区繁缕和小繁缕群体的研究

繁缕(Stellaria media)和小繁缕(S.apetala)是两个形态相似的近缘种,有人把后者作为前者的亚种或变种来处理。本文通过对南京地区不同生境的三个自然群体和三个人工控制栽培群体的取样,以群体为单位,分别测算了叶、萼片、雄蕊、花瓣、果实和种子的8个数量性状的变异,绘制了多角形图;对花粉粒和种子进行了扫描;还通过花蕾套袋试验对种子活力作了检查。结果发现繁缕和小繁缕都是近亲繁殖植物,在形态上区别明显,对生态环境的要求基本相同,但小繁缕似更能耐受人为的践踏和刈割。     

陕西蓝田公王岭“蓝田伟猴”化石的再研究

蓝田公王岭动物群中,唯一的一种非人灵长类化石由胡长康、齐陶(1978)定名为Megamacaca lantianensis(蓝田伟猴)。但按其形态,我们觉得把它归于疣猴亚科比较适宜。特别是与该亚科中的金丝猴属(Rhinopithecus)更为相像,例如蓝田标本下颌支与下颌体垂直,冠状突略向后弯,齿尖起伏较大等都显示了金丝猴的一般性质。至此,本文将蓝田伟猴归于金丝猴属,保留原有种名:Rhinopithecus(Megamacaca)lantianensis(Hu and Qi)。时代为早更新世晚期。     

Acetylcholine receptor in a C2 muscle cell variant is retained in the endoplasmic reticulum

We have examined the properties and intracellular localization of acetylcholine receptors in the C2 muscle cell line and in a variant (T-) that accumulates AChR intracellularly. On immunoblots, the subunit structures of the AChR from wild-type and T- cells were similar except that the gamma and delta subunits of the variant AChR had altered mobilities. Digestion with endoglycosidases H and F demonstrated that this difference results from a failure of high-mannose N-linked oligosaccharides on AChR subunits to be processed to complex forms in the variant. N-linked glycosylation of other proteins in the variant was normal. When examined by immunocytochemistry, the distribution of internal AChR in wild-type cells was consistent with a location both in the endoplasmic reticulum and in the Golgi. Variant cells, however, showed no evidence of Golgi staining. Subcellular fractionation experiments also demonstrated AChR in the Golgi fractions of wild-type cells, but not in those derived from T- cells. We conclude that in T- myotubes most of the AChR fails to be transported out of the endoplasmic reticulum.     

Neotypification of the genusTrichosporon

The currently accepted type species of the genusTrichosporon Behrend isT. beigelii. This species has formerly been regarded as identical toT. cutaneum. However, these fungi are now known to represent separate species with different ecology. The first species described inTrichosporon wasT. ovoides, an agent of human white piedra. A neotype strain is designated for this species, while a lectotype strain is indicated forT. cutaneum. The nameT. beigelii is considered as doubtful and consequently cannot be maintained.     

Transcobalamin II--cobalamin binding sites are present on rabbit germ cells.

Specific binding sites for rabbit transcobalamin II have been found on isolated adult rabbit germ cells. Scatchard analysis revealed a single class of binding sites for [57Co]cyanocobalamin-transcobalamin II with an association constant (Ka) of 1.3 x 10(10) M-1 and 700 sites per cell. Binding was reversible, saturable and calcium dependent. Electron microscope radioautography following incubation with iodinated transcobalamin II at 4 degrees C led to a detectable labeling mainly restricted to the plasma membrane.     

Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum.

Upon induction with heparin, Flavobacterium heparinum synthesizes and secretes into its periplasmic space heparinase I (EC 4.2.2.7), heparinase II, and heparinase III (heparitinase; EC 4.2.2.8). Heparinase I degrades heparin, and heparinase II degrades both heparin and heparan sulfate, while heparinase III degrades heparan sulfate predominantly. We isolated the genes encoding heparinases II and III (designated hepB and hepC, respectively). These genes are not contiguous with each other or with the heparinase I gene (designated hepA). hepB and hepC were found to contain open reading frames of 2,316 and 1,980 bp, respectively. Enzymatic removal of pyroglutamate groups permitted sequence analysis of the amino termini of both mature proteins. It was determined that the mature forms of heparinases II and III contain 746 and 635 amino acids, respectively, and have calculated molecular weights of 84,545 and 73,135, respectively. The preproteins have signal sequences consisting of 26 and 25 amino acids. Truncated hepB and hepC genes were used to produce active, mature heparinases II and III in the cytoplasm of Escherichia coli. When these enzymes were expressed at 37 degrees C, most of each recombinant enzyme was insoluble, and most of the heparinase III protein was degraded. When the two enzymes were expressed at 25 degrees C, they were both present predominantly in a soluble, active form.