鸭跖草属一新变型

本文发表了鸭跖草属-新变型,即白花鸭跖草Commelina communis L.f.alba Ti Chen f.nov.     

杏属一新变种和变型

本文发表了杏属一新变种和变型,即溆浦杏Armeniaca holosericea(Batal.)Kost.var.xupuensis T.Z.Li和大果辽杏A.mandshurica(Maxim.)Skv.f.major T.Z.Li     

野山楂一新变型

本文发表野山楂一新变型,即重瓣野山楂Crataegus cuneata Sieb.et Zucc.f.pleniflora S.X.Qian。     

中国黑三棱属新种和稀有植物

本文发表了中国黑三棱属二新种及一新纪录种,即细茎黑三棱Sparganium tenuicaule D.Yu et Li-hua Liu、多脊黑三棱Sparganium multiporcatum D.Yu和北方黑三棱(新拟)Sparganium hyperboreum Laest.ex Beurl.。     

东北黑三棱属新植物

本文发表了中国东北黑三棱属三新种及我国三新记录种, 三新种为东北黑三棱Sparganium manshuricum D.Yu;周氏黑三棱的Sparganium choui D.yu和抱茎黑三棱Sparganium amplexicaulium D.Yu。我国三新记录种为塔果三棱(新拟)Sparganium polyedrum Asch.et Gr.;旋序黑三棱(新拟)Sparganium glehnii Meinsh, 和日本黑三棱(新拟)Sparganium japonicum Roth.     

中国蔷薇科新植物

本文发表了蔷薇种二新种、一新变种、一新变型,即峨眉无尾果Coluria omeiensis Ku,sp.nov.;灌县花楸Sorbus guanxianensis Ku,sp.nov.;光柱无尾果Coluria omeiensis Ku var.nanzhengensis Yü et Ku.var.nov,;单花无尾果Coluria longifolia Maxim.f.uniflora Ku,f.nov.     

空心泡一新变种

本文发表了悬钩子属一新变种, 即无刺空心泡Rubus rosaefolius Smith var.inermis Z.X.Yu.     

黑三棱属一新种

本文发表了黑三棱属一新种,即弓杆黑三棱Sparganium arcuscaulis D.Yu et G.T.Yang。     

甘肃合欢属一新变型

本文发表了甘肃合欢属一新变型, 即天水合欢Albizia julibrissin flurazz.f.tianshuiensis T.S.Yao.     

安徽省苔草属（灰帽苔草组）新分类群

本文发表了安徽省苔草属(Carex)灰帽苔草组(Sect.Praecoces Christ)6新种,1新变型,即:截喙苔草Carex truncatirostris及其变型无喙苔草f.erostris,安徽苔草C.anhuiensis,宣城苔草C.xuanchengensis,祁门苔草C.qimenensis,齐云苔草C.qiyunensis和太湖苔草C.taihuensis。     

Isolation of eukaryotic ribosomal proteins. Purification and characterization of the 60 S ribosomal subunit proteins L4, L5, L7, L9, L11, L12, L13, L21, L22, L23, L26, L27, L30, L33, L35', L37, and L39.

The proteins of the large subunit of rat liver ribosomes were separated into seven groups by stepwise elution from carboxymethylcellulose with LiCl at pH 6.5. Seventeen proteins (L4, L5, L7, L9, L11, L12, L13, L21, L22, L23, L26, L27, L30, L33, L35', L37, and L39) were isolated from three of the groups (B60, D60, G60) by ion exchange chromatography on carboxymethylcellulose and by filtration through Sephadex. The amount of protein obtained varied from 0.5 to 15 mg. Eight of the proteins (L9, L11, L13, L21, L22, L35', L37 and L39) had no detectable contamination; the impurities in the others were no greater than 9%. The molecular weight of the proteins was estimated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate; the amino acid composition was determined.     

The complete primary structure of ribosomal proteins L1, L14, L15, L23, L24 and L29 from Bacillus stearothermophilus

The amino acid sequences of ribosomal proteins L1, L14, L15, L23, L24 and L29 from Bacillus stearothermophilus have been completely determined. This has been achieved by sequence analyses of peptides derived from enzymatic digestions of the proteins with trypsin, chymotrypsin, pepsin, Staphylococcus aureus protease, and Armillaria mellea protease as well as by chemical cleavage with hydroxylamine and cyanogen bromide. Based on the primary structures of the six proteins, their secondary structures were predicted using four different computer prediction programs. A comparison of the amino acid sequences of the studied proteins from B. stearothermophilus with the homologous proteins from Escherichia coli revealed that in four proteins (L1, L15, L24 and L29) between 40-50% of the residue in the sequences are identical, whereas this value is significantly higher (69%) for L14 and lower (28%) for L23. The distribution of those amino acid residues which are identical in the corresponding proteins from the two bacteria is not random along the protein chain: some regions are highly conserved whereas others are not. This finding indicates that the regions which are conserved during evolution are important for the spatial structure and/or function of the protein.     

Molecular phylogenies based on ribosomal protein L11, L1, L10, and L12 sequences

Summary Available sequences that correspond to the E. coli ribosomal proteins L11, L1, L10, and L12 from eubacteria, archaebacteria, and eukaryotes have been aligned. The alignments were analyzed qualitatively for shared structural features and for conservation of deletions or insertions. The alignments were further subjected to quantitative phylogenetic analysis, and the amino acid identity between selected pairs of sequences was calculated. In general, eubacteria, archaebacteria, and eukaryotes each form coherent and well-resolved nonoverlapping phylogenetic domains. The degree of diversity of the four proteins between the three groups is not uniform. For L11, the eubacterial and archaebacterial proteins are very similar whereas the eukaryotic L11 is clearly less similar. In contrast, in the case of the L12 proteins and to a lesser extent the L10 proteins, the archaebacterial and eukaryotic proteins are similar whereas the eubacterial proteins are different. The eukaryotic L1 equivalent protein has yet to be identified. If the root of the universal tree is near or within the eubacterial domain, our ribosomal protein-based phylogenies indicate that archaebacteria are monophyletic. The eukaryotic lineage appears to originate either near or within the archaebacterial domain. Correspondence to: P. Dennis     

Localization of proteins L4, L5, L20 and L25 on the ribosomal surface by immuno-electron microscopy

Summary Ribosomal proteins L4, L5, L20 and L25 have been localized on the surface of the 50S ribosomal subunit of Escherichia coli by immuno-electron microscopy. The two 5S RNA binding proteins L5 and L25 were both located at the central protuberance extending towards its base, at the interface side of the 50S particle. L5 was localized on the side of the central protuberance that faces the L1 protuberance, whereas L25 was localized on the side that faces the L7/L12 stalk. Proteins L4 and L20 were both located at the back of the 50S subunit; L4 was located in the vicinity of proteins L23 and L29, and protein L20 was localized between proteins L17 and L10 and is thus located below the origin of the L7/L12 stalk.     

Sequence of the amino-terminal region of rat liver ribosomal proteins S4, S6, S8, L6, L7a,L18, L27, L30, L37, L37a,and L39

The sequence of the amino-terminal region of eleven rat liver ribosomal proteins–S4, S6, S8, L7a, L18, L27, L30, L37a, and L39 - was determined. The analysis confirmed the homogeneity of the proteins and suggests that they are unique, since no extensive common sequences were found. The N-terminal regions of the rat liver proteins were compared with amino acid sequences in Saccharomyces cerevisiae and in Escherichia coli ribosomal proteins. It seems likely that the proteins L37 from rat liver and Y55 from yeast ribosomes are homologous. It is possible that rat liver L7a or L37a or both are related to S cerevisiae Y44, although the similar sequences are at the amino-terminus of the rat liver proteins and in an internal region of Y44. A number of similarities in the sequences of rat liver and E coli ribosomal proteins have been found; however, it is not yet possible to say whether they connote a common ancestry.     

Direct Organogenesis and Plant Regeneration in Preconditioned Tissue Cultures of Lathyrus cicera L., L. ochrus (L.)DC. and L. sativus L.

This study demonstrates the importance of preconditioning ofsource tissue in regeneration of multiple shoot buds from severalspecies of Lathyrus. Preconditioned multiple shoots of Lathyruscicera L., L. ochrus (L.) DC. and L. sativus L. were obtainedby germinating seeds on Murashige and Skoog (MS) medium containing50 µM N⁵-benzylaminopurine (BAP) for 2 to 3 weeks. Multipleshoot bud formation occurred when epicotyl explants of preconditionedshoots were cultured on MS medium containing 5–50 µMBAP. No shoot regeneration was observed from epicotyl explantswhich were obtained from non-preconditioned shoots. Shoot budswere formed directly on explants without an intervening callusphase after 2 to 3 weeks of culture. Regenerated shoot budsformed healthy shoots which developed prolific and strong rootswhen transferred to MS medium supplemented with 2.5 µMnaphthaleneacetic acid (NAA). Lathyrus cicera L., L. ochrus (L.) DC., Ochrus Vetch, L. sativus L., Lathyrus pea, de novo differentiation, epicotyl, preconditioning with BAP