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A Popular History of the British Ferns and the Allied Plants : Comprising the Club-Mosses, Pepperworts and Horsetails /
(1855) Moore, T. E.
The Publisher of the ' Phycologia Britannica,' considering thai 3 re-issue of that work in a cheaper and more compendious form would be ac- <;eptable to many collectors of
Popular Garden Botany; Containing a Familiar and Scientific Description of Most of the Hardy and Half-Hardy Plants Introduced into the Flower Garden
(1855) Catlow, Agnes
An admirable and cheap little volume, abounding in good illustrations of the plants that afford articles of food or applicable to purposes of manufacture. This should be on the table of every family, and its contents familiar with all rising minds."
XXXIII.—The Action of Isothiocyanates on the Aldehyde-Ammonias
(1888) Dixon, Aug. E.
Aug. E. Dixon, J. Chem. Soc., Trans., 1888, 53, 411 DOI: 10.1039/CT8885300411
A Mission Hospital in Turkey
(1913) North, R.
Computation of the Stability of Slopes
(1958) Meyer, Otto H.
Complexity of computations associated with solutions which have followed form of establishing equilibrium equations, where stresses result from weight of material lying above assumed rupture surface and resisting forces are those of Coulomb's law; new simplified solution based on assumption that circular rupture arc passes through toe of slope and at edge of crown.
Closure to “Computation of the Stability of Slopes”
(1959) Meyer, Otto H.
Characteristics of TCA Cycle of Cycloheximide-Resistant Mutant ofZygosaccharomyces Soja
(1963) Tsukada, Yoji; Sugimori, Tsunetake
Glucose catabolism in Zygosaccharomyces soja was carried out. through fermentation, whereas riboflavin producing mutant obtained by cycloheximicie treatment was found to utilize oxidative mechanisms. For instance, growth of mutant was sustained in minimal medium containing TCA cycle intermediates as the sole carbon source, whereas the mother strain could not grow on such culture media. Furthermore, malonate inhibited the oxidation of succinate with resting cells of mutant. As these results support the existence of TCA cycle in mutant, various enzyme activities relating to TCA cycle were investigated by the use of cell-free extracts of both strains. Aconitase, α-ketoglutaric decarboxylase, succinic dehydrogenase, fumarase, isocitritase and glyoxylic reductase were not detected in mother strain. These data indicated that both the TCA cycle and glyoxylate cycle did not operate in mother strain. On the other hand, all enzyme activities relating to TCA cycle and glyoxylate cycle were verified in mutant. This finding indicates that both the TCA cycle and glyoxylate cycle performed a main role in carbohydrate catabolism in mutant. The evidence that alteration of the mode of glucose catabolism from fermentation in case of mother strain to respiration of mutant elicited by the action of cycloheximicie was thus explained.
Induction of Auxotrophic Mutants from Candida Species and Their Application to <scp>l</Scp> -Threonine Fermentation
(1971) Tsukada, Yoji; Sugimori, Tsunetake
Attempts were made to induce auxotrophic mutants from Candida yeasts by ultraviolet light or ethylmethanesulfonic acid. Among Candida species tested, C. pelliculosa and C. guilliermondii var. membranaefaciens showed higher mutation rate than haploid strain of S. cerevisiae. More than 80% of the auxotrophic mutants of C. guilliermondii var. membranae-faciens were characterized to be amino acid-less, whereas a quarter of C. pelliculosa mutant was nucleic acid base-less. Accumulation of l-threonine by auxotrophic mutants derived from C. guilliermondii var. membranaefaciens by UV-irradiation was studied. One of the isoleucine auxotrophs, strain 150–4, accumulated 1.8 mg l-threonine per ml of cane molasses medium, while a tryptophan and isoleucine double auxotroph, strain P120–1, accumulated 2.0 mg per ml of the same medium. Enhancement of threonine accumulation was accomplished by methionine auxotrophs derived from strain P120-1. About 4 mg/ml of l-threonine were accumulated by one of the triple auxotrophs (try- ileu- met-), strain MB-21, after 4 days culture in 25% cane molasses medium supplemented with 1.5% urea, 10−3m l-isoleucine, 10−4m l-methionine and 10−3m anthranilic acid.
Purification and Properties of α-D-Galactosidase Produced by Corticium Rolfsii
(1972) Kaji, Akira; Yoshihara, Osamu
An α-d-galactosidase was purified from the culture filtrate of Corticium rolfsii IFO 6146 by a combination of QAE-Sephadex A-50 and SE-Sephadex C-50 chromatography. The purified enzyme was demonstrated to be free of other possibly interfering glycosidases and glycanases. The maximum activity of the enzyme towards p-nitrophenyl α-d-galactopyrano-side was found to be at pH 2.5 to 4.5, and the enzyme was fairly active at pH 1.1 to 2.0. The enzyme was stable over a pH range 4.0 to 7.0 at 5°C for 72 hr and relatively unstable at pH 1.1 to 2.0 as compared with endo-polygalacturonase, α-l-arabinofuranosidase and β-d-galactosidase produced by C. rolfsii. The enzymic activity was completely inhibited by Hg2+ and Ag+ ions, respectively. Km values were determined to be 0.16 × 10−3 m for p-nitrophenyl α-d-galactopyranoside and 0.26 × 10−3m for o-nitrophenyl α-d-galactopyranoside. The values of Vmax were also determined to be 26.6 μmoles and 28.6 μmoles per min per mg for p- and o-nitrophenyl α-d-galactopyranoside, respectively.
Purification and Properties of α- <scp>d</Scp> -Galactosidase Produced by Corticium Rolfsii
(1972) Kaji, Akira; Yoshihara, Osamu
An α-d-galactosidase was purified from the culture filtrate of Corticium rolfsii IFO 6146 by a combination of QAE-Sephadex A-50 and SE-Sephadex C-50 chromatography. The purified enzyme was demonstrated to be free of other possibly interfering glycosidases and glycanases. The maximum activity of the enzyme towards p-nitrophenyl α-d-galactopyrano-side was found to be at pH 2.5 to 4.5, and the enzyme was fairly active at pH 1.1 to 2.0. The enzyme was stable over a pH range 4.0 to 7.0 at 5°C for 72 hr and relatively unstable at pH 1.1 to 2.0 as compared with endo-polygalacturonase, α-l-arabinofuranosidase and β-d-galactosidase produced by C. rolfsii. The enzymic activity was completely inhibited by Hg2+ and Ag+ ions, respectively. Km values were determined to be 0.16 × 10−3 m for p-nitrophenyl α-d-galactopyranoside and 0.26 × 10−3m for o-nitrophenyl α-d-galactopyranoside. The values of Vmax were also determined to be 26.6 μmoles and 28.6 μmoles per min per mg for p- and o-nitrophenyl α-d-galactopyranoside, respectively.
Improved Microbial Production of Colominic Acid, a Homopolymer of N-Acetylneuraminic Acid
(1973) Uchida, Yoshihiro; Tsukada, Yoji; Sugimori, Tsunetake
A culture medium has been devised for producing colominic acid in improved yields. Major improvements were obtained by using sorbitol as a source of carbon, by adding phosphate in high concentrations, and by supplementing a limited amount of yeast extract. E. coli O 16: Kl: HNM produced approximately 3000 µg/ml of colominic acid on cultivation at 37°C for 46 hr with a liquid medium consisting of sorbitol (2.0%), (NH4)2SO4 (0.5%), K2HPO4 (1.4%), MgSO4·7H2O (0.05%), and yeast extract (0.05%). Isolation and purification by deproteinization with ammonium sulfate, precipitation with ethanol, and by column chromatography on anion exchange resins resulted in a pure colominic acid preparation devoid of internal ester linkages. In producing colominic acid, strains forming S-type colonies were more active than those forming R-type colonies.
Distribution of Neuraminidase in Arthrobacter and Its Purification by Affinity Chromatography1
(1977) Uchida, Yoshihiro; Tsukada, Yoji; Sugimori, Tsunetake
Neuraminidase [sialidase, EC 3.2.1.18] was found to be widely distributed in bacteria belonging to Arthrobacter. Among these bacteria, Arthrobacter ureafaciens, A. oxydans, and A. aurescens produced relatively potent neuraminidase activities. For the production of this enzyme, not only colominic acid, a homopolymer of N-acetylneuraminic acid, but also N-acetylneuraminic acid, the reaction product of this enzyme, are effective as sources of carbon. An affinity adsorbent specific for neuraminidase was prepared by cross-linking colominic acid with soluble starch by means of epichlorohydrin. Neuraminidase from A. ureafaciens could be purified on this affinity column. The purified neuraminidase was shown to be free from protease, N-acetylneuraminic acid aldolase, phospholipase C, and glycosidases. Aminoff's assay procedure for sialic acid was modified to avoid the centrifugation step. The modified procedure gave a higher molecular extinction coefficient.
Purification and Properties of Acid Pectinesterase from Corticium Rolfsii.
(1977) Kaji, Akira; Matsuo, Takaharu; Yoshihara, Osamu
A pectinesterase was purified from the culture filtrate of C. rolfsii IFO 6146 by a combination of salting out, gel filtration on Sephadex G-100 and chromatography on DEAE-Sephadex A-50, SP-Sephadex C-50 and hydroxylapatite. The purified enzyme was found to be homogeneous protein by ultracentrifugal analysis. The molecular weight of the purified enzyme was found to be about 37, 000 by the gel filtration. The enzyme was stable over the pH range of 1.1 to 10.0 and retained 90% of its activity when stored at pH 1.1 at 5°C for 72 hr. The maximum activity occurred at pH 2.5 to 4.5 at 45°C. The enzyme was fairly active at a very low pH (1.1) or low temperature (10°C). Hg2+ was a potent inhibitor. The enzyme was active not only on high molecular pectin methyl esters but also on low molecular esters. The high enzymatic activity at very low pH values and the unusual tolerance to hydrogen ions are characteristics of pectinesterase from C. rolfsii. The enzyme is one of the acid esterases.
Lymphocyte Neuraminidase Activity and Sialic Acid Concentration in Normal Subjects
(1982) Taniuchi, Koji; Doi, Kunihiro; Ohashi, Kumiko; Miyamoto, Yoshinobu; Yamaguchi, Nobuo; Chifu, K; Sugimori, Tsunetake
An Endo-1,5-.ALPHA.-L-Arabinase, Which Can Disintegrate Potato Tissue.
(1983) Kaji, Akira; Yoshihara, Osamu
An endo-1, 5-α-L-arabinase [EC 3.2.1.99] has been highly purified from the culture fluid of Bacillus subtilis IFO 3022 grown on a medium containing beet pulp extract. The molecular weight of the enzyme was 33, 000 by SDS polyacrylamide gel electrophoresis. The purified enzyme was active on 1, 5-arabinan, and inactive on p-nitrophenyl α-L-arabinofuranoside. The optimum pH was 6.0. The enzyme was inhibited by Hg2+, but not by L-arabonic-γ-lactone. The purified enzyme was able to loosen potato tissue.
Production, Purification and Characterization of HYI, an Antiyeast Substance, Produced by Hansenula Saturnus.
(1984) Ohta, Yasuhiro; Tsukada, Yoji; Sugimori, Tsunetake
An anti-yeast substance, HYI, was produced by Hansenula saturnus. Production of HYI under aerobic incubation conditions took place in parallel with yeast cellular growth. HYI was concentrated by ultra filtration from the culture filtrate and purified by ion-exchange chromatography followed by gel filtration. It was then crystallized. HYI migrated as a single protein band on sodium dodecyl sulfate/polyacrylamide gel electrophoresis and had a molecular weight of about 8500. Anthrone positive compounds could not be detected in HYI. The isoelectric point ofHYI was pH 5.80±0.05. The activity ofHYI was unaffected by heating at 60°C for 1 hr. It showed a broad anti-yeast spectrum.
Distribution of N-Acetylneuraminate Lyase in Bacteria and Its Production by Escherichia Coli.
(1985) Uchida, Yoshihiro; Tsukada, Yoji; Sugimori, Tsunetake
Bacteria capable of producing N-acetylneuraminate lyase (N-acetylneuraminic acid aldolase, EC 4.1.3.3) were sought by using a culture medium containing N-acetylneuraminic acid as a sole source of carbon. The enzyme was found to be distributed in a veriety of bacteria belonging to such genera as Pseudomonas, Escherichia, Aerobacter, Proteus, Micrococcus, Sarcina, Brevibacterium, Corynebacterium, Arthrobacter, Bacillus and Bacterium. No bacteria secreted the enzyme into the medium. Substantially N-acetylneuraminate lyase of bacteria seems to be an intracellular enzyme. Potent N-acetylneuraminate lyase activities were detected in all of the strains belonging to Escherichia such as E. coli, E. freundii and E. intermedia. There was no difference in the enzyme production between a strain of E. coli which had the ability to produce colominic acid and one which had lost the ability.
La Villita Earthworks (41BX677): San Antonio, Texas A Preliminary Report of Investigations of Mexican Siege Works at the Battle of the Alamo
(1986) Labadie, Joseph H.
La Villita Earthworks is located in the heart of downtown San Antonio, Texas. The site appears to have been formed initially in late February 1836, by Mexican soldiers with General Santa Anna’s invading forces during the second battle of the Alamo. The outcome of this battle has been the topic for literally thousands of books over the past 149 years. Now, for the first time, archaeological evidence has been discovered which provides the first real glimpse at the Mexican side of the battle of the Alamo. The ramifications of the discovery are yet to be fully realized. Military historians and other scholars now have material evidence from the actual battle by which to evaluate the accuracy of the several eyewitness accounts of the battle. For archaeologists, the site represents the most comprehensive look yet afforded at San Antonio during this famous period.
Organizing a Local Lake Management Program
(1986) Anderson, Raymond L.; Adams, Mike; O’connor, William P.; Mcvoy, Richard S.; Kasierski, Bernard; Stowe, Randolph J.; Spencer, Dean
(1986). ORGANIZING A LOCAL LAKE MANAGEMENT PROGRAM. Lake and Reservoir Management: Vol. 2, No. 1, pp. 426-430.
Demonstrationsfreiheit - Eine Kontroverse - Ein Vorschlag Zur Dogmatischen Neukonstruktion Des Grundrechts Aus Art. 8 GG Als Recht Auf undefinedOrdnungsstörungundefined
(1987) Ladeur, Karl‐heinz
Die Konstruktion des Grundrechts der Versammlungsfreiheit bereitet seit jeher Schwierigkeiten, weil seine dogmatische Eigenstndigkeit ~wischen zwei dogma-