Eutrophication and succession of phytoplankton in reservoir of Korea - monthly variations of plankton community in Lake Soyang

The community of plankton and the environmental factors were investigated in Lake Soyang from January to July 1994. The relationship between transparency and biovolume of phytoplankton was negatively correlated. Phytoplankton dominants in Lake Soyang were Anabaena spp., Microcystis aeruginosa, Asterionella formosa, Asterionella gracillima Melosira distans, Synedra acus, and Asterococcus limneticus, Zooplankton dominants were Polyarthra spp., Keratella spp., Asplanchna placentula, Bosmina coregoni, and Daphnia longispona. Phytoplankton and zooplankton were clearly related each other with respect to biovolume, not to numbers. Microcystis aeruginosa rapidly increased and Daphnia longirostris disappeared in July, because Microcystis aeruginosa secret toxic substances to Daphnia longirostris. Transparency decreased from January to June, but increased in July. The highest number of phytoplankton was obserbed in April, and one month later, the zooplankton reached a maximal level in population density, implicating that spring bloom of phytoplankton was good feeding condition for zooplankton.Article信州大学理学部附属諏訪臨湖実験所報告 9: 175-186(1995)departmental bulletin pape

教職支援センターからみた学生支援の変遷

departmental bulletin pape

帆付き風車 : 『失楽園』における驚異の表象

2012-10-11departmental bulletin pape

作物チーム

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Distribution of phenotypic characteristics of the mutant population and rate of pleiotropy

Number of M2 families in each phenotypic group. The x-axis indicates the nine major phenotypic categories, listed in Table 2, and the y-axis indicates the total number of M2 families. Each bar represents the number of mutants in the corresponding category. The blue bar represents the quantity of pleiotropic mutants (having more than one phenotype), given by the first number in the category label. The red bar represents the non-pleiotropic mutants and is given by the second number in the category label. Total number of M2 families (y-axis) sharing 1-5 major phenotypic categories (x-axis). The bar for one phenotypic category indicates how many mutants are categorized in only one phenotypic group (non-pleiotropic mutants), and the bars for the 2-5 phenotypic categories represent the number of mutants that share two to five phenotypes, respectively. In each case, the total number of mutants is indicated on the top of the bar.<p><b>Copyright information:</b></p><p>Taken from "UTILLdb, a forward and reverse genetics tool"</p><p>http://genomebiology.com/2008/9/2/R43</p><p>Genome Biology 2008;9(2):R43-R43.</p><p>Published online 26 Feb 2008</p><p>PMCID:PMC2374714.</p><p></p

Identification of a <i>TI1/TI2</i> double null mutant in a pea germplasm collection.

<p>(<b>a</b>) Multiplex screening of pea germplasm DNA for seed protein gene variants. The predicted <i>TI2</i> amplicon evident in top and lower panels is highlighted with an arrow; this amplicon is absent from the line analysed in the middle panel: JI 262. (<b>b</b>) <i>TI2</i> sequence amplified from JI 262. The 14 bases missing are indicated with dashes, leading to a premature stop codon (red font). (<b>c</b>) Predicted amino acid sequence of the mutant JI 262 genes, compared with wild-type TI1 and TI2; the premature stop codons (*) occur within the 42 amino acid pre-pro-peptide (region affected by the mutation highlighted pink). Primer-encoded amino acids in italics; predicted amino acid sequences beyond deletions underlined; variant amino acids highlighted. (<b>d</b>) TIA of the mutant, JI 262, and a mutant F2 segregant compared with a wild-type F2 segregant from a cross between JI 262 and cv. Cameor (J x C). For comparison, the C77Y mutant and control lines (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0134634#pone.0134634.g002" target="_blank">Fig 2</a>) are plotted alongside. TIU per unit meal (left), per unit protein (right).</p

Enzyme inhibitory profile of the TI1 E109K mutation.

<p>Seed proteins from wild-type and mutant lines from the TI1 E109K family were separated by cation-exchange chromatography. Absorbance profiles at 280 nm are shown (a, b: red and blue lines without symbols; mAbs, left-hand scale). Using BAPNA and BTEE as specific substrates, the trypsin (<b>a</b>) and chymotrypsin inhibitory (<b>b</b>) activities of wild-type (red triangle) and mutant (blue triangle) protein fractions are shown, relative to assays where trypsin activity is 100% (control; right-hand scale). Numbers in peaks in each chromatogram correspond to the different forms of TI1 and TI2 (peak 1: TI2 processed; Peak 2: TI2 unprocessed; Peak 3: TI1 processed; Peak 4: TI1 unprocessed. (<b>c</b>) in-gel protease inhibitory activity of inhibitor isoforms from wild-type (i, iii) and E109K mutant (ii, iv) lines. Zymogram blue casein gels were treated with the digestive enzymes, trypsin (i, ii) or chymotrypsin (iii, iv); dark areas indicate where the enzyme has been inhibited. The direction of electrophoresis on non-denaturing gels is indicated (-, +). The arrow indicates the position of the isoform that is missing from the mutant lines (tracks ii and iv).</p

Missense <i>TI1</i> gene mutants obtained by TILLING and used in this study.

<p>Changes in encoded proteins are shown, and the BC2F3 and BC2F4 lineage identifiers for mutant and corresponding wild-type mutant alleles. Mutation positions for genes and proteins are given relative to the initiator methionine codon or amino acid, respectively.</p><p>Missense <i>TI1</i> gene mutants obtained by TILLING and used in this study.</p

Impact of mutations on enzyme inhibition.

<p>Trypsin (TIU, <b>a, c</b>) and chymotrypsin (CIU, <b>b, d</b>) inhibitory units per mg of meal (<b>a, b</b>) or per mg of protein (<b>c, d</b>) of three TILLING mutants (C77Y, S85F, E109K) and their corresponding wild-type pea lines. For each plot, significant differences (p < 0.01) between wild-type and mutant lines within each pair are denoted (a, b, as appropriate on bars in each chart).</p

Impact of mutations on TI1 structure.

<p>(<b>a</b>) Homology model of TI1, a major Bowman-Birk inhibitor from pea. The trypsin (blue) and chymotrypsin (red) inhibitory domains are shown, with the identity and location of the mutations indicated by cyan spheres and the disulphide bonds in green. N and C refer to the amino- and carboxy-terminal ends, respectively. (<b>b</b>) Amino acid sequence deduced from the <i>TI1</i> gene from the pea cultivar Cameor. The sequences of the inhibitory domains are underlined and the positions of the seven disulphide bonds are indicated with connecting lines. The disulphide bond affected by the mutation C77Y is highlighted in blue. K and Y at position P1 (*) determine specificity for trypsin and chymotrypsin, respectively. Letters and numbers in red indicate the positions of the mutations shown in (a). Amino acid numbers are based on the protein coding region of the gene, which includes a 42 amino acid pre-pro-peptide; carboxy-terminal processing removes the last nine amino acids from a subset of TI proteins in vivo.</p