Subcellular localization and drug-Induced changes; of rat liver and kidney esterases

1968 ◽  
Vol 46 (2) ◽  
pp. 207-212 ◽  
Author(s):  
W. S. Schwark ◽  
D. J. Ecobichon
Keyword(s):  
Rat Liver ◽  
Gel Electrophoresis ◽  
Esterase Activity ◽  
Microsomal Fraction ◽  
Starch Gel Electrophoresis ◽  
Drug Induced ◽  
Liver Esterase ◽  
Liver And Kidney ◽  
Starch Gel ◽  
Induced Changes

The subcellular distribution of the esterases of rat liver and kidney was examined by differential centrifugation followed by quantitative titrimetric analysis, starch-gel electrophoresis, and electron microscopy of the subcellular fractions. The esterases were found primarily in the microsomal fraction of the cell. Soluble or cytoplasmic forms of esterases were also found. These conclusions were substantiated by induction studies with DDT and sodium phenobarbitone. Both drugs were capable of inducing liver esterase activity, DDT being more potent. In contrast to the liver, increased kidney esterase activity was not induced by these compounds.

A Comparison of the Relative Amounts of Tissue Esterases in Liver and Kidney Homogenates

1963 ◽  
Vol 46 (5) ◽  
pp. 863-868
Author(s):  
Sheila I Read ◽  
W P Mckinley
Keyword(s):  
Sex Difference ◽  
Gel Electrophoresis ◽  
Rabbit Kidney ◽  
Starch Gel Electrophoresis ◽  
Liver And Kidney ◽  
Starch Gel ◽  
Liver Homogenates

Abstract The relative amounts of the ali-esterases in beef and rabbit kidney and liver homogenates have been evaluated quantitatively, after resolution of the esterases by starch-gel electrophoresis. The relative amounts of total ali-esterases in livers and kidneys of a number of animals and fowl have been determined. The data presented and other unpublished data show that the ali-esterase content of tissues increases with age and that there is a sex difference.

scholarly journals ELECTROPHORETIC SEPARATION OF ESTERASES OF PULMONARY ALVEOLAR CELLS

1970 ◽  
Vol 18 (3) ◽  
pp. 167-177 ◽  
Author(s):  
ROBERT SCHIFF ◽  
MARY ANN BRUNSTETTER ◽  
ROBERT L. HUNTER ◽  
CARROLL E. CROSS
Keyword(s):  
Alveolar Macrophages ◽  
Gel Electrophoresis ◽  
Esterase Activity ◽  
Spectrophotometric Analysis ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Separation ◽  
Alveolar Cells ◽  
Additional Band ◽  
Female Mice ◽  
Starch Gel

Starch gel electrophoresis and vertical flat bed electrophoresis in polyacrylamide gels were used to separate butyrylesterases of pulmonary alveolar macrophages (PAMs) from RF/Al(+) and RF/Al(–) mice. PAM esterases from (+) mice showed five bands in starch and five or six in acrylamide whereas four and three or four bands, respectively, were found in extracts from (–) animals. The additional band or bands present only in positive samples corresponded to the Es-2 prealbumin serum esterase found only in the RF/Al (+) animals. This isozyme was more sensitive to diisopropylfluorophosphate than any other PAM esterase. The serum counterpart was sensitive to the same degree. None of the macrophage esterases were inhibited by eserine sulfate. Spectrophotometric analysis of serum esterase activity indicated a statistically significant increase in female mice from both sublines as compared to their respective males, but did not show a difference between the two sublines. The usefulness of the esterase marker in studies of PAM origin and pathologic conditions is discussed.

Haemolymph esterases in the female larval honeybee, Apis mellifera L., during caste development

1968 ◽  
Vol 46 (5) ◽  
pp. 1013-1017 ◽  
Author(s):  
Ram K. Tripathi ◽  
S. E. Dixon
Keyword(s):  
Apis Mellifera ◽  
Gel Electrophoresis ◽  
Esterase Activity ◽  
Starch Gel Electrophoresis ◽  
Prepupal Stage ◽  
General Increase ◽  
General Decline ◽  
Starch Gel ◽  
Caste Development ◽  
Esterase Patterns

The haemolymph esterase patterns were obtained for eight ages during larval development of the two female castes of the honeybee, Apis mellifera L., by starch gel electrophoresis. Qualitatively, the patterns differed markedly with age within and between the castes. Quantitatively, esterase activity is higher in workers up to 72 hours of age and thereafter shows a general decline, whereas in queens the activity is lower up to 72 hours of age and is followed by a general increase. In both castes the activity is slightly increased towards prepupal stage. The significance of these results is discussed in relation to female dimorphism.

INHERITANCE OF ELECTROPHORETIC VARIANTS OF SERUM ESTERASES IN DOMESTIC FOWL

1968 ◽  
Vol 10 (4) ◽  
pp. 961-967 ◽  
Author(s):  
A. A. Grunder
Keyword(s):  
Gel Electrophoresis ◽  
Esterase Activity ◽  
Domestic Fowl ◽  
Staining Intensity ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Variants ◽  
Region I ◽  
Starch Gel ◽  
The Mean

Three regions of serum esterase activity of chickens were differentiated by means of starch gel electrophoresis and appropriate stains. Regions I and II seemed to represent aliesterase while region III apparently represented a cholinesterase. The patterns of zones of region I were classified into three phenotypes named A, B, and AB and the hypothesis was proposed that these are controlled by two codominant alleles named EsA and AsB. The staining intensity of these esterase zones among adults was sex-associated in that the mean staining intensity of zones was greater in male than in female sera. Frequency of the EsB allele was 0.70, 0.76, and 0.85 in three meat lines.

Sinapine Esterase. II . Specificity and Change of Sinapine Esterase Activity During Germination of Raphanus sativus

1980 ◽  
Vol 35 (11-12) ◽  
pp. 963-966 ◽  
Author(s):  
Dieter Strack ◽  
Gerhild Nurmann ◽  
Gesine Sachs
Keyword(s):  
Enzyme Activity ◽  
Gel Electrophoresis ◽  
Esterase Activity ◽  
Raphanus Sativus ◽  
Lag Phase ◽  
Starch Gel Electrophoresis ◽  
Rapid Degradation ◽  
Choline Esters ◽  
Starch Gel ◽  
Naphthyl Acetate

Abstract Following a 20 to 24 h lag-phase after sowing, the onset of both rapid degradation of sinapine (sinapolycholine) and rapid increase in sinapine esterase activity in cotyledons of Raphanus sativus was observed. After 2 days of germination maximal enzyme activity was reached and declined in subsequent germination stages as rapidly as it had appeared. Esterases, active against indophenyl acetate, showed highest activity in dry seeds, declining to more than 50% between the 1st and 3rd day of germination. Starch gel electrophoresis showed that all protein extracts contained a multiplicity of esterases, active against α-naphthyl acetate. When gels were incubated with sinapine, one new band appeared, stainable with diazotized ρ-nitroaniline. This band represents sinapine esterase activity. Tests for substrate specificity towards cinnamic acid choline esters showed highest enzyme activity with sinapine. Studies on the occurrence of sinapine esterase in other Brassicaceae revealed that the enzyme activity coincides with the occurrence and degradation of sinapine.

scholarly journals Properties of ribosomal proteins from two mammalian sources

1967 ◽  
Vol 102 (3) ◽  
pp. 735-741 ◽  
Author(s):  
P. Cohn
Keyword(s):  
Hydrochloric Acid ◽  
Glutamic Acid ◽  
Rat Liver ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Protein Fractions ◽  
Starch Gel Electrophoresis ◽  
Guanidinium Chloride ◽  
Starch Gel ◽  
Rabbit Reticulocytes

1. Ribosomal protein fractions from rabbit reticulocytes and rat liver were prepared by extracting ribosomes with 0.2n-hydrochloric acid or guanidinium chloride and subsequent dialysis. 2. Treatment for 2.5hr. or less with 0.2n-hydrochloric acid dissolved 46-54% of the proteins, which were richer in arginine and lysine and in N-terminal alanine groups and poorer in aspartic acid and glutamic acid and in N-terminal glycine groups than the acid-insoluble proteins. 3. Protein fractions prepared from the guanidinium chloride extract of ribosomes from rat liver were usually more basic than those from rabbit reticulocytes. 4. The ratios lysine: arginine of fractions in the guanidinium chloride extracts were appreciably higher for proteins from rabbit reticulocytes than from rat liver. 5. The concentration of urea and the pH of the gel affected the rate of migration and number of bands in starch-gel electrophoresis.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

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