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.

Detection of multiple forms of proteolytic enzymes by starch gel electrophoresis

1968 ◽  
Vol 46 (10) ◽  
pp. 1317-1320 ◽  
Author(s):  
E. kaminski ◽  
W. Bushuk
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Direct Detection ◽  
Proteolytic Enzymes ◽  
Urea Concentration ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Separation ◽  
Multiple Forms ◽  
Starch Gel ◽  
Sensitive Method

A rapid and sensitive method for the direct detection of multiple forms of proteolytic enzymes by starch gel electrophoresis is described. The location of the enzyme components is identified by the degradation of hemoglobin which is included in the starch gel. This method was used to identify the enzyme components of the 10 commercial proteolytic enzymes bromelain, chymotrypsin, ficin, papain, pepsin, pronase B, protease, proteinase, and two preparations of trypsin. The effects of urea concentration and the ionic strength of aluminium lactate buffer were also examined. The best results were obtained with 3 M urea and with an ionic strength of 0.1 for the lactate buffer. It was observed that the number of enzyme components decreased with increasing concentrations of urea or increasing ionic strength of lactate buffer. The number of enzyme components did not always correspond to the number of protein bands. Self-digestion occurred in some of the protein bands in the starch gel after electrophoretic separation of the proteolytic enzymes.

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.

HETEROGENEITY OF INSULIN: II. CHROMATOGRAPHY OF INSULIN ON CARBOXYMETHYL CELLULOSE IN UREA CONTAINING BUFFERS

1967 ◽  
Vol 45 (2) ◽  
pp. 221-237 ◽  
Author(s):  
W. W. Dillon ◽  
R. G. Romans
Keyword(s):  
Gel Electrophoresis ◽  
Carboxymethyl Cellulose ◽  
Anomalous Behavior ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Separation ◽  
Minor Components ◽  
Starch Gel ◽  
Starch Gels ◽  
Cellulose Column

Chromatography of insulin, on carboxymethyl (CM) cellulose columns in urea-containing buffers, revealed the presence of at least five components, one major and four minor, in commercial insulin. This fractionation is related to other chromatographic fractionations of insulin and the nature of the minor components is discussed.Insulin which had been incubated in HCl was chromatographed. The behavior of the incubated products on the column showed that two or more amide groups were hydrolyzed simultaneously but at different rates. Because of the anomalous behavior of one of the components, it is postulated that a group other than the amides is also transformed during acid incubation. This component is present in commercial insulin samples.The electrophoretic separation of insulin in urea–starch gels was shown to be due to charge differences on the molecules rather than size differences. Correlation of the components separated on the CM-cellulose column with those separated in the urea–starch gel electrophoresis showed that much smaller charge differences on the molecules are distinguished on the CM-cellulose column than in the gel.

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.

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.

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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