Agricultural Activities of a Meadow Eliminated Plant Litter from the Periphery of a Farmland in Inner Mongolia,China

The purpose of our investigation was to clarify the effects of agriculture on the process of loss of litter at the periphery of a farmland. This study revealed the generation process of an ecologically unusual phenomenon that is observed around cropland in semi-arid regions. We hypothesized that the vegetation around a farmland cannot supply plant litter to the ground surface because the ecological structure has been changed by agricultural activities. The study was conducted at Xilingol steppe, Xilingol League, Inner Mongolia Autonomous Region, China. Four study lines were established from the edge of an arable field to the surrounding meadow and parallel to the wind direction during the strong wind season. Key measurement for each line was set at the border between the farmland and steppe. Four study sites were set at intervals along each line. Plant litter, soil particle size distribution, plant species composition, plant volume, and species diversity were investigated. Despite using the same mowing method at the meadows of all study sites, the litter at the only periphery of the farmland completely disappeared. Soil particle size distribution in steppe, which was adjacent to the farmland, was similar to that of the farmland. Plant community structure at the periphery of the farmland was different from that of the far side from the farmland. This implies that soil scattered from the farmland affected the species composition of the steppe. Consequently, the change in plant community structure induced litter loss because of mowing. We concluded that plant litter was lost near the farmland because of the combined effects of farming and mowing. The results support our hypothesis that the vegetation around a farmland cannot supply plant litter because the ecological structure has been changed by agricultural activities.     

Isolation and Chemical Structure of New Oxidation Product of 5-Ketogluconic Acid,and a Hypothetical Pathway from Glucose to Tartaric Acid through this New Compound

In the course of study on the mechanism of the tartaric acid formation from 5-ketogluconic acid, a new intermediary substance with mauve color to Abdel-Akhel and Smith’s reagent was isolated from intact cell culture liquid. The chemical structure of this substance was determined as 1,2-dihydroxyethyl hydrogen L(+) tartrate from the results of hydrolysis experiments and from the identifications of the constituents of the molecule, and named “pretaric acid.” Tartaric acid was evidently produced from pretaric acid by intact cell culture. Clearly, then, pretaric acid appears to be an intermediate in the formation of tartaric acid from 5-ketogluconic acid. The authors assumed that in the formation of pretaric acid from 5-ketogluconic acid, a Baeyer-Villiger type oxidation occurred.     

A cellular 3,3',5-triiodo-L-thyronine binding protein from a human carcinoma cell line. Purification and characterization

A cellular binding protein for 3,3',5-triiodo-L-thyronine (T3) was solubilized with 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate (CHAPS) from A431 human epidermoid carcinoma cells. The binding activity is T3 specific. Analysis of the equilibrium binding data indicated that the binding protein has one class of binding sites for T3 with a Kd of (17 +/- 3) nM and Bmax of (1.8 +/- 0.6) pmol/50 micrograms of protein. The pH optimum for binding is 6.8. The T3 binding protein elutes from Sephadex G-200 in an included peak which has a Stokes radius of 40 A and sediments on glycerol gradients at 3.7 S. By affinity labeling with [3,5-125I]thyroxine a protein with a molecular weight of 58,000 was specifically labeled. Its isoelectric point was determined to be 7.1, which is different from the reported pIs of other thyroid hormone binding proteins. p58 was successively purified to apparent homogeneity by chromatography on Sephadex G-200, QAE-Sephadex, SP-Sephadex, and hydroxylapatite. Approximately 50 micrograms of purified protein was obtained from 2.5 X 10(9) cells with a yield of 1.1%. The purified protein retains its binding activity. The specific binding activity is enriched by approximately 1000-fold. With the availability of a purified protein with T3 binding activity, it becomes possible to study its cellular function.     

Methylation strongly enhances DNA bending in the replication origin region of the Escherichia coli chromosome

Summary Two-dimensional gel electrophoresis, at high and low temperatures, and gel mobilities of circularly permuted DNA segments showed a large bending locus about 50 bp downstream from the right border of the 245 by oriC box, a minimal essential region of autonomous replication on the Escherichia coli chromosome. Bending was strongly enhanced by Dam methylation. In DNA from a Dam^– strain, the mobility anomaly arising from altered conformation was much reduced, but was raised to the original level by methylation in vivo or in vitro. Enhancement of the mobility anomaly was also observed by hybrid formation of the Dam^– strand with the Dam⁺ strand. Near the bending center, GATC, the target of Dam methylase, occurs seven times arranged essentially on the same face of the helix with 10.5 by per turn. We concluded that small bends at each Dam site added up to the large bending detectable by gel electrophoresis.     

A cytoplasmic thyroid hormone binding protein: characterization using monoclonal antibodies

We have previously purified a cellular thyroid hormone binding protein (p58) from a human carcinoma cell line [Kitagawa, S., Obata, T., Hasumura, S., Pastan, I., & Cheng, S.-y. (1987) J. Biol. Chem. 262, 3903-3908]. In the present study, the binding characteristics, the molecular properties, and subcellular localization of p58 were further characterized. Binding of the purified p58 to thyroid hormones was examined. Analysis of binding data indicates that p58 binds to 3,3',5-triiodo-L-thyronine (T3) with a Kd of 24.3 +/- 0.3 nM and n = 0.71. p58 binds to L-thyroxine similarly as to T3. However, D-T3 and reverse-T3 bind to p58 with an affinity 4- and 20-fold less than that of T3, respectively. By use of the purified p58 as an immunogen, two hybridomas, J11 and J12, secreting monoclonal antibodies to p58 were isolated; both antibodies belong to the IgG1K subclass. J12 recognizes p58 from human, monkey, dog, hamster, and rat, but not mouse. J11 exhibits a similar species specificity except that it does not react with p58 from hamster. With these antibodies, p58 was found to be not posttranslationally modified by glycosylation, sulfation, or phosphorylation. It has a cellular degradation rate t1/2 congruent to 2.1 h. Immunocytochemical studies indicate that p58 is located in the nonmembranous cytoplasm (cytosol). These results are consistent with subcellular fractionation studies which show that greater than 95% of J11 and J12 reactivity and T3 binding activity can be found in the 110,000g supernatant.     

Salt tolerance of the reed plant Phragmites communis

Reed plants ( Phragmites communis Trinius) were grown at NaCl concentrations up to 500 m M and their growth, mineral contents and leaf blade osmotic potential were determined. Addition of NaCl up to 300 m M did not affect growth significantly. Sucrose, Cl^-and Na⁺ concentrations in the shoots increased with the salinity of the medium and the shoot water content decreased. K⁺ always contributed most to the leaf osmotic potential. Even in the presence of 250 m M NaCl in the rooting medium, the leaf blade contained only 50 mM Na⁺, suggesting that the plants have an efficient mechanism for Na⁺ exclusion. ²²Na⁺ uptake experiments suggested that the retranslo-cation of absorbed Na⁺ from shoots to the rooting medium lowered the uptake of Na⁺.     

Immuno-Gold Localization of Nitrogenase in Root Nodules of Elaeagnus pungens Thunb

The molybdenum-iron component of nitrogenase (Mo-Fe component)was purified from soybean nodule bacteroids and antibody wasraised against it in rabbits. Antibody raised against the 53kDa polypeptide which was the major protein in the Mo-Fe componentfraction of soybean nitrogenase was confirmed to be specificto the nitrogenase by immunodiffusion and immunotitration. Thenitrogenase from root nodules of Elaeagnus pungens cross-reactedwith the antibody and appeared from the results of the immunodiffusionto be partially identical to soybean nitrogenase. Using the antibody, we examined intracellular localization ofnitrogenase in root nodules of Elaeagnus pungens, in which Frankiais present as a symbiont, by immuno-gold labelling. Thin sectionsof nodules of Elaeagnus pungens were first treated with anti-nitrogenasespecific antibody and then with colloidal gold-protein A asa marker. The gold particles were observed to be concentratedin the vesicles of the endophyte Frankia. This provides strongsupport for the existence E of nitrogenase in the vesicles.Furthermore, our results suggested that nitrogenase localizesin the hyphae of the endophyte Frankia in Elaeagnus pungensnodules. ¹Present address: Iwata Experiment Station, Japan Tobacco Inc.,Iwata-gun, Shizuoka 438, Japan. (Received March 9, 1988; Accepted July 28, 1988)