scholarly journals Oxime Reactivation of Diethylphosphoryl Human Serum Cholinesterase

1967 ◽  
Vol 242 (11) ◽  
pp. 2683-2687
Author(s):  
E.I.C. Wang ◽  
P.E. Braid
Keyword(s):  
Human Serum ◽  
Serum Cholinesterase

Chemical composition, antimicrobial, antioxidative and anticholinesterase activity of Satureja Montana L. ssp montana essential oil

2014 ◽  
Vol 9 (7) ◽  
pp. 668-677 ◽  
Author(s):  
Tatjana Mihajilov-Krstev ◽  
Dragan Radnović ◽  
Dušanka Kitić ◽  
Vesna Jovanović ◽  
Violeta Mitić ◽  
...  
Keyword(s):  
Essential Oil ◽  
Essential Oils ◽  
Human Serum ◽  
Biological Activities ◽  
Serum Cholinesterase ◽  
Health Improvement ◽  
Chemical Compositions ◽  
Bacterial Strains ◽  
Antimicrobial Potential ◽  
Satureja Montana

AbstractThe present study investigates the chemical compositions of three Satureja montana L. ssp montana essential oils and correlates chemical variability with biological activities. GC/MS analysis showed that with an increase in altitude (100–500–800 m), a higher content of linalool, terpinen-4-ol and cis-sabinene hydrate was found, while the percentage of phenolic compounds, thymol and carvacrol decreased. Antimicrobial activity of the essential oils was tested against 7 fungal and 23 bacterial strains. The essential oil characterized by the highest content of phenols and alcohols exhibited the highest antimicrobial potential. The correlation analysis showed that the major carriers of the obtained antioxidant activity are oxygenated monoterpenes. All essential oils inhibited human serum cholinesterase activity. High antimicrobial potential, together with moderate antioxidant capacity and strong inhibition of human serum cholinesterase, classifies S. montana essential oil as a natural source of compounds that can be used in the treatment of foodborne and neurological diseases, wound and other infections, as well as for general health improvement.

Ultrasonic Effects on lsoenzymes

1966 ◽  
Vol 12 (4) ◽  
pp. 181-186 ◽  
Author(s):  
Clyde A Dubbs
Keyword(s):  
Human Serum ◽  
Ultrasonic Treatment ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Serum Cholinesterase ◽  
Starch Gel Electrophoresis ◽  
Selective Activation ◽  
Intracellular Enzymes ◽  
Starch Gel

Abstract Several significant effects of ultrasonic treatment on human serum cholinesterase and aminopeptidase isoenzymes and on other serum proteins have been found by starch gel electrophoresis. The selective activation of one cholinesterase isoenzyme is especially striking. These effects must be considered when ultrasonic treatment is used for the extraction of intracellular enzymes. When the effects are appreciated, ultrasonics should provide a valuable tool for isoenzyme research.

A METHOD FOR THE DETECTION OF ATYPICAL FORMS OF HUMAN SERUM CHOLINESTERASE. DETERMINATION OF DIBUCAINE NUMBERS

1957 ◽  
Vol 35 (6) ◽  
pp. 339-346 ◽  
Author(s):  
W. Kalow ◽  
K. Genest
Keyword(s):  
Human Serum ◽  
Local Anaesthetic ◽  
Phosphate Buffer ◽  
Esterase Activity ◽  
Experimental Temperature ◽  
Serum Cholinesterase ◽  
Good Discrimination ◽  
Esterase Inhibition ◽  
Recording Spectrophotometer

Cases with atypical esterase activity were found by determining esterase inhibition in numerous sera. A suitable inhibitor was the local anaesthetic dibucaine (cinchocaine, TN Nupercaine, Perkain). A good discrimination between typical and atypical sera was obtained under the following conditions: The esterase activity of human serum diluted 1:100 was measured with a recording spectrophotometer at 240 mμ. The substrate was 5 × 10−5 M benzoylcholine dissolved in M/15 phosphate buffer, pH 7.4. The concentration of the inhibitor was 10−5 M. With the experimental temperature around 25 °C, the average inhibition of the typical enzyme was 78.8 ± 0.3%. The inhibition of the atypical esterases was less; in rare cases the inhibition was only 16%. For each person, the inhibition characteristics were constant over a period of several months, and independent of the esterase level. The degree of inhibition measured under these conditions and expressed in per cent has been termed "Dibucaine Number".

A METHOD FOR THE DETECTION OF ATYPICAL FORMS OF HUMAN SERUM CHOLINESTERASE. DETERMINATION OF DIBUCAINE NUMBERS

1957 ◽  
Vol 35 (1) ◽  
pp. 339-346 ◽  
Author(s):  
W. Kalow ◽  
K. Genest
Keyword(s):  
Human Serum ◽  
Local Anaesthetic ◽  
Phosphate Buffer ◽  
Esterase Activity ◽  
Experimental Temperature ◽  
Serum Cholinesterase ◽  
Good Discrimination ◽  
Esterase Inhibition ◽  
Recording Spectrophotometer

Cases with atypical esterase activity were found by determining esterase inhibition in numerous sera. A suitable inhibitor was the local anaesthetic dibucaine (cinchocaine, TN Nupercaine, Perkain). A good discrimination between typical and atypical sera was obtained under the following conditions: The esterase activity of human serum diluted 1:100 was measured with a recording spectrophotometer at 240 mμ. The substrate was 5 × 10−5 M benzoylcholine dissolved in M/15 phosphate buffer, pH 7.4. The concentration of the inhibitor was 10−5 M. With the experimental temperature around 25 °C, the average inhibition of the typical enzyme was 78.8 ± 0.3%. The inhibition of the atypical esterases was less; in rare cases the inhibition was only 16%. For each person, the inhibition characteristics were constant over a period of several months, and independent of the esterase level. The degree of inhibition measured under these conditions and expressed in per cent has been termed "Dibucaine Number".

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