Light-induced variation in the growth and dynamics of transplanted ramets of the understory herb,Aster acuminatus

Summary Ramets of the understory herb, Aster acuminatus, were transplanted from two source populations into eight understory garden sites that varied in light and soil moisture levels. Ramet growth, clonal growth, flowering and survivorship were monitored for three growing seasons. Large differences among gardens in ramet growth, clonal growth and flowering developed in the first growing season and increased in the next two years. This variation was positively correlated with garden light level but not at all with soil moisture. Mortality rates were low in all gardens and showed that genets from any particular source could survive over a broad range of environmental conditions. There was no conclusive evidence for any source population differences in the capacity to survive or grow in different environments. The rapid, light-induced responses of transplanted ramets resulted in garden populations very similar in appearance to natural populations experiencing similar light regimes. These results combined with those from other studies of A. acuminatus provide strong evidence for the importance of light in explaining population patterns and dynamics in this species.     

Modulation of cyclic nucleotide-independent protein kinase from chick intestine by naturally occurring polyamines and mucopolysaccharides

Summary Chick duodenal mucosa contains an endogenous factor which is capable to inhibit selectively a homologous polyamine-sensitive protein kinase. The inhibitor was partially purified and characterized, and it was found to contain typical mucopolysaccharidic components.Glycosidases digestion studies, selective degradation analysis and spectrophotometric titrations with metachromatic dyes indicated that the inhibitor preparation contained two major moieties identified as heparin-like and heparan sulfate-like structures. In chick intestine the inhibitor was specific for polyamine-sensitive protein kinase since selectively interacted with it and was inert towards other cAMP-independent and cAMP-dependent protein kinases. The inhibitory effect of the endogenous factor was counteracted by naturally occurring polyamines such as spermine. The order of potency of various polyamines was: spermine > thermine spermidine diamines. The release of inhibition by addition of physiological concentrations of spermine was also apparent when using cytosolic proteins as endogenous phosphate acceptors. These results suggest that a possible role of polyamine in the regulation of polyamine-sensitive protein kinase in the intestine is to protect the enzyme from the inhibitory action of endogenous heparinoids.     

Dilution and acidification effects during the spring flood of four Swedish mountain brooks

The seasonal variation in water chemistry was followed during 1980 and 1981 in four mountain brooks in the southern part of Swedish Lapland. In the area investigated the soil is calcareous and the brook water is very well buffered during the major part of the year, with alkalinity varying between 0.4 and 1.0 milliequivalents per liter and with pH values about 7.5. These years the snow had a pH of approximately 5.2, which was considerably higher than has been reported from adjacent areas in the lower, coniferous region. During snowmelt the water discharge increased drastically, and although the net transport of bicarbonate increased, alkalinity showed low values due to dilution with meltwater. pH decreased, but not further than to 6.3–6.5, far from values reported in 1979 (pH less than 5), apparently due to the comparatively clean snow. A slight deficit in alkalinity, as compared to the nonmarine calcium and magnesium content, points to an acidification impact on the area. During maximum runoff some chemical variables, like aluminium, iron, nitrogen and phosphorus, behaved reversely to what might be expected during dilution and reached maxima in concentrations. It is concluded that the extreme runoff characteristics of high mountain areas make brook water more sensitive to acid precipitation than might be expected when regarding only the calcareous properties of soil and bedrock.     

Volatile constituents of the leaves of Cupressus dupreziana and Cupressus sempervirens

The essential oils of the leaves of Cupressus dupreziana and Cupressus sempervirens were compared. The composition of the hydrocarbon fraction showed a great similarity between the two species.     

Comparative Hydrolysis of Sphingomyelin and 2-N-(Hexadecanoyl)-Amino-4-Nitrophenyl-Phosphorylcholine by Normal Human Brain Homogenate at Acid and Neutral pH

Hydrolysis of sphingomyelin and 2-N-(hexade-canoyl)-amino-4-nitrophenyl-phosphorylcholine (HDA-PC), a synthetic analogue of sphingomyelin, by acid and Mg-dependent neutral sphingomyelinases was tested with a homogenate of normal human brain cortex. Results demonstrated quite different substrate specificities for these enzymes. Acid sphingomyelinase, which is neither activated by MgCl₂ nor inhibited by EDTA, hydrolyzed both substrates (the hydrolysis ratio of HDA-PC to sphingomyelin is ?2). In contrast, Mg-dependent neutral sphingomyelinase, which is inhibited by EDTA and reactivated by MgCl₂, hydrolyzed only sphingomyelin (the hydrolysis ratio of HDA-PC to sphingomyelin is ?0-0.05). This synthetic substrate seems to be useful for selective determination of acid sphingomyelinase and for avoiding interference of Mg-dependent neutral sphingomyelinase.     

Taxonomic Implications of Spore Fine Structure in Clostridium bifermentans

Thirty-five strains of Clostridium bifermentans were, in most part, culturally homogeneous by conventional taxonomic criteria but were heterogeneous with respect to spore fine structure. Fourteen of the strains produced spores with appendages, distributed among four distinct ultrastructural types. No consistent correlation existed between spore type and other variable properties of these strains. It is proposed, therefore, that these spore appendage-type strains be considered as "varieties" of C. bifermentans and that they should not be designated as new species.     

Structural Genes for a Newly Recognized Acetolactate Synthase in Escherichia coli K-12

Evidence is reported that shows the presence in Escherichia coli K-12 of a newly found acetolactate synthase. This enzyme is the product of two genes, ilvH and ilvI, both located very close to leu. Amber mutations have been found in both genes and therefore their products are polypeptides. Mutations in the ilvH gene cause the appearance of an acetolactate synthase activity which is relatively resistant to valine inhibition and can be separated by adsorption on hydroxylapatite from another activity present in the extract and more sensitive to valine inhibition than the former. A mutant altered in the ilvI gene was isolated among the revertants sensitive to valine inhibition of an ilvH mutant. Such a mutant lacks the resistant acetolactate synthase. A temperature-sensitive revertant of the ilvI mutant contained a temperature-sensitive acetolactate synthase. Thus ilvI is the structural gene for a specific acetolactate synthase. The activity of the ilvH gene product has been measured by adding an extract containing it to a purified ilvI acetolactate synthase, which, upon incubation, became more sensitive to valine inhibition. Conversely, a valine-sensitive acetolactate synthase (the product of the ilvH and the ilvI genes) became more resistant to valine inhibition upon incubation with an extract of a strain containing a missense ilvH gene product.     

The isolation and properties of phenylalanine hydroxylase from human liver

Phenylalanine hydroxylase was prepared from human foetal liver and purified 800-fold; it appeared to be essentially pure. The phenylalanine hydroxylase activity of the liver was confined to a single protein of mol.wt. approx. 108000, but omission of a preliminary filtration step resulted in partial conversion into a second enzymically active protein of mol.wt. approx. 250000. Human adult and full-term infant liver also contained a single phenylalanine hydroxylase with molecular weights and kinetic parameters the same as those of the foetal enzyme; foetal, newborn and adult phenylalanine hydroxylase are probably identical. The K(m) values for phenylalanine and cofactor were respectively one-quarter and twice those found for rat liver phenylalanine hydroxylase. As with the rat enzyme, human phenylalanine hydroxylase acted also on p-fluorophenylalanine, which was inhibitory at high concentrations, and p-chlorophenylalanine acted as an inhibitor competing with phenylalanine. Iron-chelating and copper-chelating agents inhibited human phenylalanine hydroxylase. Thiol-binding reagents inhibited the enzyme but, as with the rat enzyme, phenylalanine both stabilized the human enzyme and offered some protection against these inhibitors. It is hoped that isolation of the normal enzyme will further the study of phenylketonuria.