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  • Monkey diaphragm  (1)
  • Nitrogen fixation  (1)
  • cerebral ischemia  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Influence of a carbamate pesticide on growth, respiration (14C)-carbon metabolism and symbiosis of aRhizobium sp. (1979)
    Springer
    Plant and soil 51 (1979), S. 355-361 
    Details
    ISSN: 1573-5036
    Keywords: Aldicarb ; 14C-carbon metabolism ; Cowpea ; Growth ; Nitrogen fixation ; Nodulation ; Pesticide ; Respiration ; Rhizobium ; Soil ; Symbiosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary Addition of aldicarb (2 methyl-2(methyl thio) propionaldehyde-0-methyl carbamoyl oxime) in the growth medium enhanced the growth ofRhizobium sp. (cowpea group) at 2 ppm level while an inhibition was observed at the normal (5 ppm) and higher (10 ppm) concentrations. Respiration of the cells was also inhibited by 5 and 10 ppm levels of the chemical eventhough a stimulation was observed at 2 ppm (lower) concentration. The insecticide, when incorporated at 5 and 10 ppm levels in the medium increased the14C-glucose incorporation and considerably altered the assimilation of the radioactive carbon in different fractions of rhizobium cells. Soil application of this insecticide (Temik 10 G) reduced the number of nodules formed and the total nitrogen content in cowpea plants inoculated with theRhizobium sp. but enhanced the dry matter production of cowpea plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02197782
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation of a tripeptide (Ala-Gly-Ser) exhibiting weak acetylthiocholine hydrolyzing activity from a high-salt soluble form of monkey diaphragm acetylcholinesterase (1992)
    Springer
    Neurochemical research 17 (1992), S. 351-359 
    Details
    ISSN: 1573-6903
    Keywords: Monkey diaphragm ; acetylcholinesterase ; limited tryptic digestion ; tripeptide ; acetylthiocholine hydrolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A high-salt soluble form of acetylcholinesterase (AChE) was purified from monkey (Macaca radiata) whole diaphragm by a two step affinity chromatographic procedure using m-aminophenyl trimethylammoniumchloride hydrochloride-Sepharose and procainamide-Sepharose columns. The purified enzyme showed three major protein bands at 80 kDa, 78 kDa and 60 kDa on SDS-gel electrophoresis. [3H]Diisopropyl fluorophosphate ([3H]DFP) labeled enzyme also gave three radioactive peaks corresponding to these three bands. The purified enzyme pretreated with dithiothreitol and subjected to limited trypsin digestion gave a peptide fragment of molecular weight ∼300 Da showing weak acetylthiocholine hydrolyzing activity as identified by Sephadex G-25 gel filtration. Sequence analysis showed that the active peptide fragment was a tripeptide with the sequence Ala-Gly-Ser. When the purified AChE was labeled with [3H]DFP, digested with trypsin and subjected to Sephadex G-25 chromatography, a radioactive peak that would correspond to the tripeptide fragment was seen. The kinetics, inhibition characteristics and binding characteristics to lectins of the active peptide fragment was compared with the parent enzyme. A synthetic peptide of sequence Ala-Gly-Ser was also found to exhibit acetylthiocholine hydrolyzing activity. The kinetics and inhibition characteristics of the synthetic peptide was similar to those of the peptide derived from the purified enzyme, except that the synthetic peptide was more specific towards acetylthiocholine than butyrylthiocholine. The specific activity (units/mg) of the synthetic peptide was about 29480 times less than that of the purified AChE.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00974577
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Free fatty acids, lipid peroxidation, and lysosomal enzymes in experimental focal cerebral ischemia in primates: Loss of lysosomal latency by lipid peroxidation (1988)
    Springer
    Neurochemical research 13 (1988), S. 193-201 
    Details
    ISSN: 1573-6903
    Keywords: Lysosomal enzymes ; lipid peroxidation ; cerebral ischemia ; monkey brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Experimental focal cerebral ischemia was produced in monkeys (Macaca radiata) by occlusion of the right middle cerebral artery (MCA). The release of the lysosomal glycosidases, β-d-hexosaminidase, α-l-fucosidase and α-d-mannosidase into the soluble fraction in the right basal ganglia of the experimental animals was measured at different periods from 30 min to 12 hr after occlusion and compared with the corresponding sham operated control animals. There was a significant increase in the released lysosomal enzymes in the MCA occluded animals at all periods and particularly at 4 hr after occlusion. The CSF from the experimental animals also showed elevated levels of hexosaminidase and fucosidase. The free fatty acids (FFA) measured in the basal ganglia at 30 min and 2 hr after occlusion showed a 100 fold increase in the experimental animals. The predominant fatty acid released was linoleic acid (18:2) followed by arachidonic acid (20:4). Lipid peroxidation in the basal ganglia measured by the thiobarbituric acid (TBA) reaction in the presence or absence of ascorbic acid also showed a significant increase in the experimental animals at all periods with a maximum at 30 min to 2 hr after occlusion. In order to assess whether lipid peroxidation causes damage to the lysosomes and release of the enzymes, a lysosome enriched P2 fraction from the normal monkey basal ganglia was prepared and the effect of peroxidation studied. Maximum peroxidation in the P2 fraction was observed in the presence of arachidonic acid, ascorbic acid and Fe2+. There was a good correlation between the extent of lipid peroxidation and the in vitro release of lysosomal hexosaminidase from the P2 fraction. Anti-oxidants which strongly inhibited lipid peroxidation in the P2 fraction prevented the release of hexosaminidase. The results suggested that in ischemia produced by MCA occlusion lipid peroxidation which damages the lysosomal membrane causes the release of lysosomal hydrolytic enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00971532
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    Paper (German National Licenses)
    Fulltext
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