Fibrous substances in tobacco leaves are the main precursors of acetaldehyde, propionaldehyde, acrolein, acetone, methylethylketone, diacetyl, methanol, furan, an unknown compound, No. 6 and an unknown compound, No. 16 in cigarette smoke.
Sugars in tobacco leaves are the main precursors of 2-methylfuran and 2,5-dimethyl- furan in cigarette smoke.
Resinous substances in tobacco leaves are the main precursors of isoprene and an unknown compound, No. 2 in cigarette smoke.
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A removed ear, not yet mature, exerts a depressing effect upon the development of the stem and ucon the leaf's functions.
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The threads and the pistils removed inhibit the enlongament of the stem and alter the functions of leaves.
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Maturing seeds removed cause trubles on the function of the vegetative organ.
1. Zenker's solution 4 hours at 37°C or Dominici's 3 hours.
2. 70% alcohol, 12 to 18 hours at room temperature.
3. 80% alcohol, about 5 to 6 hours.
4. 90% alcohol, about 4 to 6 hours.
5. Absolute alcohol about 16 hours.
6. Ether and absolute alcohol aa, about 8 hours.
7. 16 to 24 hours in the following mixture: celloidin 1 g., methyl salycilate 25 cc., abs. alcohol 25 cc., ether 25 cc.
8. Chloroform and paraffin, 2 to 3 hours.
10. Paraffin, 1 to 1 1/2 hours.
11. Embed.
1. Cut sections 4 to 5 μ.
2. Bring section to water and cover with Lugol's iodine for 10 minutes.
3. Decolorize with a 2% sodium thiosulfate (hypo).
4. Wash thoroly with water.
5. Cover with a mixture of equal parts of 0.5% phloxine and 1% eosin Y (National Aniline brand) and leave for 15 minutes.
6. Wash with water and stain 2 to 5 minutes in 0.1% azure B (National Aniline).
7. Wash with 96% alcohol and decolorize in a mixture of 2 parts absolute alcohol with 1 part clove oil, ordinarily for not more than 1/2 to 1 minute.
8. Dehydrate rapidly, clear, and mount in Yucatan Elemi.
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the species was found in 26 localities, including all of those previously reported by other authors, and had an area of occurrence about 6 500 km2
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the population of T. ruspolii was censused by means of linear transects, giving an estimate of about 10 000 individuals.
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T ruspolii frequents mostly forest margins and relatively dry Acacia woodlands. These habitats are less severely threatened by human activity than true forests in present day Ethiopia.
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since T. ruspolii and the related T. leucotis usually occur in different habitats (the latter preferring wetter forest) competition is not likely to be a severe threat for T. tuspolii.
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the species is subject to some egg collecting by local people, but probably not to a severe extent. Other direct human persecution was not recorded.
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although there is no hint of numerical decrease in the past, this is likely to occur in the future, as consequence of the increasing human pressure in the region.
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Research into the visual shape discrimination abilities of compound‐eyed animals has almost exclusively been limited to insects, the crustaceans having been virtually ignored. The two groups have many dissimilarities, having primarily adapted in different habitats to different lifestyles. Differences may exist in visual systems and visually mediated behavior.
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Fiddler crabs (Uca pugilator), without training, differentially approached dissimilar silhouettes presented simultaneously, demonstrating visual discrimination between stationary, geometric shapes of equal‐area. The strength of response was ordered hierarchically: vertical rectangle, horizontal rectangle, triangle, square, circle.
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Basic geometric shapes were used to facilitate replication and comparison with research findings from other species.
Total concentration of soluble salts.
Relative proportion of sodium to other cations.
Concentration of boron or other toxic elements.
Under certain conditions, the bicarbonate concentration as related to the concentration of calcium plus magnesium.
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inefficiency of the purification procedure;
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surface denaturation;
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imperfect freeze-drying of the final product; and
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factors yet unknown vhich cause alteration in the immoglobulins or other protein components not ellminated by the purification procedures.
The catalase activity of Candida tropicalis pK 233 was induced by hydrocarbons but not by glucose, galactose, ethanol, acetate or lauryl alcohol.
The induction of the catalase activity depending upon hydrocarbons was sensitive to cycloheximide but not to chloramphenicol.
Glucose repressed strongly the induction of the catalase activity by hydrocarbons but galactose did not affect seriously.
When C. tropicalis was incubated with hydrocarbons, the appearance of microbodies was observed electronmicroscopicaliy.
l-Aspartate was found to replace l-asparagine in the protective action from acid inactivation of l-asparaginase (EC 3.5.1.1) produced by Escherichia coli A–1–3 and at the same time to inhibit the proteolytic inactivation by α-chymotrypsin.
l-Asparaginase changed in its chromatographic properties in the presence of l-aspartate and became to be absorbed on the CM Sephadex column.
The sedimentation patterns of l-asparaginase at pH 3.5 were identical either in the presence or absence of l-aspartate, showing partial dissociation. But the reversibility to the active state was observed only in the enzyme dissolved in the solution containing l-aspartate.
l-Aspartate did not prevent the enzyme either from the dissociation into subunits or from decrease in the activity by urea.
High concentration of l-aspartate was shown to inhibit the l-asparagine hydrolysis reaction.
l-Aspartate was suggested from ORD measurements to cause changes in the higher structure as well as the ionic properties or proteolytic inactivation.
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Determine concernsby using risk assessment techniques for various scenarios.
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Identify the consequences by systematically identifying hazards.
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Undertake calculations by using relevant models.
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Evaluate certainties, uncertainties, and probabilities involved in the calculations of the vulnerability and of the exposure.
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Compare with criteriato assess the need for further action.
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Determine and act on options to control, mitigate, and adapt to the risk.
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Communicatethe results to those who need to know.
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the activity of some glycolytic enzymes increases greatly (81% and 400% increase of, respectively, Gl-6-P-dehydrogenase and aldolase) upon incubation of dry seeds for few hours at 4 °C.
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The decrease of enzyme activity upon dehydration of seeds and the increase during the subsequent imbibition can be shown reproducibly.
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This same observation is made for oxygen uptake.
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l'archisporio è pluricellulare e possono svilupparis talvolta pi[ugrave] cellule madri;
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normalmente solo una cellula madre arriva a maturità;
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delle quattro megaspore solo una è fertile e precisamente la pi[ugrave] calazale;
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lo sviluppo del gametofito è del tipo Normale cioè Monomegasporiale con oangio emisporiale.
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Nyssodrysilla nov. gen. mit N. irrorata (Melzer) aus Brasilien als Generotype, N. viliata (Melzer), comb, nov., aus Brasilien und N. lineata nov. spec, aus Peru.
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Nyssodrysola nov. gen. mit N. stictica nov. spec. aus Peru als Generotype.
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Sciadosurus nov. gen. mit S. albobrunneus nov. spec. aus Peru als Generotype.
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Acarinozineus nov. gen. mit A. striatus nov. spec. aus Peru als Generotype und A. spinicornis nov. spec, aus Mexiko.
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Alcathousites nov. gen. mit A. chaclacayoi nov. spec. aus Peru als Generotype.
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Xylergatina nov. gen. mit X. pulcher (Lane) aus Peru als Generotype.
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Xylergatoides nov. gen. mit X. asper (Bates) aus Brasilien und Argentinien als Generotype.
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Xylergates Bates, Generotype X. lacteus (Bates), mit Beschreibung der beiden neuen Arten X. elaineae aus Peru und X. dorotheae aus Britisch‐Guayana.
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Chaetanes Bates, Generotype C. setiger (Bates), mit Beschreibung der drei neuen Arten C. costulatus aus Peru, C. nigrobasalis aus Brasilien und C. apicalis aus Französisch‐Guayana.
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Wo es erforderlich ist, sind Bestimmungstabellen gebracht und die Arten abgebildet.
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Identification of skulls
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Taxonomic situation of the vicugna
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Origin of the alpaca.
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Single interactions in chemical systems involve formation or breaking of bonds.
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Formation of a bond is always accompanied by a release of energy, and breaking a bond always requires energy.
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Energy changes in chemical processes are the net result of the breaking and formation of bonds.
The most suitable carbon source for 5-ketofructose fermentation by Gluconobacter suboxydans Strain 1 was confirmed to be d-sorbitol or l-sorbose using growing and resting cells. d-Fructose had little effect on the formation of this dicarbonylhexose.
The optimal pH for the formation from l-sorbose by intact cells was found to be at 4.2.
The activity of the pentose phosphate cycle in the resting cells was calculated as 13~17 μatoms/hr/mg of dry cells by the use of the manometric techniques.
There was no strain tested so far which could accumulate a large amount of 5- keto-d-fructose from d-sorbitol except this bacterium.
The experimental results shown in this paper makes the prediction that a certain dehydrogenating system of l-sorbose is functional in the organism, and the metabolic pathways of d-sorbitol via l-sorbose and 5-keto-d-fructose is proposed.
The egg white, thick and thin fractions, was solubilized in 1.0% SDS solution by vigorous mixing and subjected to gel filtration on a Sepharose 4B column, eluted with 1.0% SDS. The isolated thick and thin ovomucins were found by analytical disc electrophoresis to be free from contamination with lysozyme.
In the velocity sedimentation the two ovomucin fractions behave similarly, both comprising at least two components with sedimentation coefficients 35 S and 30 S.
The chemical compositions of the two ovomucin fractions showed only notable difference in that the carbohydrate content of the thick white ovomucin was somewhat higher than that of the thin white ovomucin. The amino acid profiles of the two fractions were similar.
L-Asparaginase (EC 3.5.1.1) from Escherichia coli A–l–3 was acetylated using acetic anhydride as a modifying chemical. The fully acetylated L-asparaginase retained 60% of the activity of the unmodified L-asparaginase.
The acetylated L-asparaginase hydrolyzed D-asparagine and L-glutamine as well as L-asparagine in the same ratio as the unmodified L-asparaginase did.
However, the effects of pH on the activity of the acetylated L-asparaginase showed very interesting differences from that of L-asparaginase. On the other hand, both L-asparaginase and the acetylated L-asparaginase exhibited similar pH activity curves on L-glutamine hydrolysis.
The acetylated L-asparaginase was found to become more stable against acid or heat in the presence of L-aspartate than in its absence in the same manner as L-asparaginase was.