PROPERTIES AND CLASSIFICATION OF THE SOLUBLE ESTERASES OF HUMAN BRAIN

1966 ◽  
Vol 44 (2) ◽  
pp. 225-232 ◽  
Author(s):  
D. J. Ecobichon
Keyword(s):  
Alkaline Phosphatase ◽  
Human Brain ◽  
Esterase Activity ◽  
Water Soluble ◽  
Human Tissues ◽  
Esterase Pattern ◽  
Vertical Zone ◽  
Zone Electrophoresis ◽  
Starch Gel

Water-soluble proteins and enzymes of human brain were separated by vertical zone electrophoresis in starch gel. Fifteen bands of esterase activity were detected in brain. Various substrates and inhibitors were used in efforts to identify enzymes in addition to a comparison of the esterase pattern with patterns obtained from other human tissues. One zone, composed of four bands of acetylesterase activity, was found to be common to all the tissues investigated with the exception of serum. Two bands of cholinesterase and two bands of A-esterase activity were identified. The remaining bands, which were aliesterases possessing broad overlapping substrate specificity and inhibitor sensitivity, were electrophoretically different from those of other tissues. Observations on alkaline phosphatase, acid phosphatase, and lactate dehydrogenase were recorded for comparison with the data on esterases.

CHARACTERIZATION OF THE ESTERASES FROM ELECTRIC TISSUE OF ELECTROPHORUS BY STARCH-GEL ELECTROPHORESIS

1967 ◽  
Vol 45 (7) ◽  
pp. 1099-1105 ◽  
Author(s):  
D. J. Ecobichon ◽  
Y. Israel
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Water Soluble ◽  
Starch Gel Electrophoresis ◽  
Electrophorus Electricus ◽  
Vertical Zone ◽  
Zone Electrophoresis ◽  
Starch Gel

The water-soluble esterases of a microsome-free supernatant of the electric tissue of Electrophorus electricus were separated by vertical-zone electrophoresis in starch gel. Specific and nonspecific substrates and inhibitors were used in conjunction with histochemical techniques to identify the enzymes. Acetylcholinesterase was present in the form of four bands of activity, the electrophoretic mobility of which was suggestive of aggregated forms of the enzyme. Pseudocholinesterase was detected as two weak bands of activity. A third esterase was identified as a nonspecific carboxylesterase and shown to be a sialoprotein.

PROPERTIES AND CLASSIFICATION OF THE SOLUBLE ESTERASES OF HUMAN KIDNEY

1964 ◽  
Vol 42 (2) ◽  
pp. 277-286 ◽  
Author(s):  
D. J. Ecobichon ◽  
W. Kalow
Keyword(s):  
Human Kidney ◽  
Lactic Dehydrogenase ◽  
Renal Tissue ◽  
Water Soluble ◽  
Serum Cholinesterase ◽  
Hepatic Tissue ◽  
Liver And Kidney ◽  
Starch Gel ◽  
Zone Characteristic

Water-soluble proteins and enzymes of human kidney were separated by vertical zone electrophoresis in starch gel and compared with those of human serum and liver. In most individuals 11 bands of proteins were detected with the aid of amido black B; some individuals had one additional band. Various substrates and inhibitors were used in efforts to identify enzymes. Five zones of esterase activity were found. One zone, characteristic of serum cholinesterase, was believed to be due to serum contained in the tissue. A zone of isozymic esterases was found to be common to both human liver and kidney and reacted like acetylesterase. Another zone, migrating at a rate approximating that of serum albumin, reacted like an aliesterase. Three small esterase bands, showing a marked hydrolysis of α-naphthyl butyrate, were found to be characteristic of renal tissue on comparison with hepatic tissue and serum. Observations on alkaline phosphatase, acid phosphatase, leucine aminopeptidase, lactic dehydrogenase, and catalase were recorded for comparison with the data on esterases.

PROPERTIES AND CLASSIFICATION OF THE SOLUBLE ESTERASES OF HUMAN SKELETAL AND SMOOTH MUSCLE

1965 ◽  
Vol 43 (1) ◽  
pp. 73-79 ◽  
Author(s):  
D. J. Ecobichon ◽  
W. Kalow
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Human Liver ◽  
Renal Tissue ◽  
Water Soluble ◽  
Serum Cholinesterase ◽  
Liver And Kidney ◽  
Starch Gel ◽  
Zone Characteristic

Water-soluble proteins and enzymes of human skeletal and smooth muscle were separated by vertical-zone electrophoresis in starch gel and compared with those of human liver and kidney. Thirteen bands of proteins were detected with amido black in skeletal muscle, five of which were also detected in smooth muscle. Various substrates and inhibitors were used in efforts to identify enzymes. Ten bands of esterase activity were detected in skeletal muscle, and nine in smooth muscle. One zone, characteristic of serum cholinesterase, was believed to be due to serum contained in the tissue. A zone of isozymic esterases found in skeletal and smooth muscle was similar to a zone in human liver and kidney and reacted like an acetylesterase. Other esterase bands, which showed a marked hydrolysis of α-naphthyl butyrate, were similar to aliesterases of renal tissue. Observations on alkaline phosphatase, acid phosphatase, aminopeptidase, lactate dehydrogenase, and catalase were recorded for comparison with the data on esterases.

SOME PROPERTIES OF THE SOLUBLE ESTERASES OF HUMAN LIVER

1961 ◽  
Vol 39 (9) ◽  
pp. 1329-1332 ◽  
Author(s):  
D. J. Ecobichon ◽  
W. Kalow
Keyword(s):  
Human Serum ◽  
Human Liver ◽  
Histochemical Staining ◽  
Enzymatic Properties ◽  
Water Soluble ◽  
Electrophoretic Migration ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Staining Methods

Zone electrophoresis on starch gel in conjunction with various histochemical staining methods was applied to the study of the water-soluble esterases of liver. The results indicated that in regard to electrophoretic migration and enzymatic properties, none of the human liver esterases was identical with any of the human serum esterases.

MULTIPLE FORMS OF HUMAN LIVER ESTERASES

1965 ◽  
Vol 43 (5) ◽  
pp. 595-602 ◽  
Author(s):  
D. J. Ecobichon
Keyword(s):  
Human Liver ◽  
Molecular Size ◽  
Water Soluble ◽  
Electrical Charge ◽  
Multiple Forms ◽  
Substrate Specificities ◽  
Graphic Analysis ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Relative Retardation

Zone electrophoresis in starch gel of the water-soluble human liver esterases resulted in the separation of three zones of activity, each composed of several bands. The relative sizes of the enzymes in each zone were studied by utilizing the relative retardation of the electrophoretic migration induced by changes in the concentration of starch. On the basis of graphic analysis, four esterase bands comprising the zone migrating towards the cathode were found to be similar in molecular size or shape. A similar observation was made for seven bands comprising a zone migrating towards the anode. Taken with the substrate specificities and sensitivities toward various inhibitors, these observations strengthen the hypothesis that at least two of the hepatic esterases, an acetylesterase and an aliesterase, exist as multiple forms, differing primarily in net electrical charge.

CHARACTERIZATION OF RAT LIVER AND KIDNEY ESTERASES

1967 ◽  
Vol 45 (4) ◽  
pp. 451-455 ◽  
Author(s):  
W. S. Schwark ◽  
D. J. Ecobichon
Keyword(s):  
Female Rats ◽  
Electrophoretic Separation ◽  
Male And Female ◽  
Male And Female Rats ◽  
Vertical Zone ◽  
Zone Electrophoresis ◽  
Liver And Kidney ◽  
Starch Gel ◽  
Inhibition Studies

Vertical zone electrophoresis in starch gel was employed in conjunction with various histochemical techniques to characterize the liver and kidney esterases of male and female rats. Tissue-specific patterns were observed for each organ and a sex-dependent difference was noted on electrophoretic separation of the liver extracts. On the basis of substrate specificity and inhibitor sensitivity, both organs were observed to contain similar nonspecific aliesterases or carboxylesterases (EC 3.1.1.1). Inhibition studies showed the presence of two types of aliesterase in the liver and kidney extracts.

Separation of alkaline phosphatase isoenzymes from human kidney and comparison with alkaline phosphatases from other human tissues, urine, and Escherichia coli.

1983 ◽  
Vol 29 (1) ◽  
pp. 100-106 ◽  
Author(s):  
A W Hodson
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Molecular Mass ◽  
Gel Filtration ◽  
Human Kidney ◽  
Human Tissues ◽  
Ammonium Sulfate Precipitation ◽  
Alkaline Phosphatases ◽  
Alkaline Phosphatase Isoenzymes ◽  
Starch Gel

Abstract Human kidney isoenzymes of alkaline phosphatase (EC 3.1.3.1) after extraction with butan-1-ol were separated by ammonium sulfate precipitation, gel filtration, and chromatofocusing fractionation methods. The separation at each fractionation step was monitored by starch gel and equilibrium-gradient-pore electrophoresis, the latter technique also being used to determine molecular mass. The determined molecular mass (daltons) of alkaline phosphatase from human placenta was 132 000, from urine 95 000, and three isoenzymes from kidney were 195 000, 140 000, and 95 000, respectively. The mass of Escherichia coli alkaline phosphatase was 80 000 daltons, and that of human liver alkaline phosphatase was assumed to be 160 000 daltons. The urinary isoenzyme and the electrophoretically fastest migrating kidney isoenzyme were similar with regard to pH optima, charge, and molecular mass as well as response to L-phenylalanine, L-homoarginine, heat, and urea. Bacterial alkaline phosphatase could be distinguished from the alkaline phosphatases in human tissues and urine by differences in the response to changes in pH and several other physicochemical properties.

HYDROLYTIC ENZYMES IN BOVINE SKELETAL MUSCLE: I. STARCH GEL ELEGTROPHORETIC SEPARATION AND PROPERTIES OF SOLUBLE ESTERASES

1965 ◽  
Vol 43 (11) ◽  
pp. 1779-1786 ◽  
Author(s):  
H. F. MacRae ◽  
C. J. Randall
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscles ◽  
Hydrolytic Enzymes ◽  
Water Soluble ◽  
Heat Stable ◽  
Heat Labile ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Bovine Skeletal Muscle ◽  
Naphthyl Acetate

Water-soluble esterases of certain bovine skeletal muscles were separated by horizontal zone electrophoresis in starch gel in a discontinuous ouffer system. Eighteen bands of esterase activity were detected by the use of α-naphthyl acetate and α-naphthyl butyrate as substrates. Other substrates and various inhibitors were used to characterize the separated enzymes. A group of presumed isozymic esterases (three bands), which hydrolyzed α-naphthyl butyrate but not any other substrate tested, was sensitive to organophosphates, was heat labile, and was classified as aliesterase or, more specifically, as butyrylesterase. Another group of presumed isozymic esterases (four bands) hydrolyzed only α-naphthyl acetate and indoxyl acetates, was heat stable and resistant to organophosphates, and was tentatively classified as arylesterase or cathepsin. Eleven heat-labile esterase bands hydrolyzed both α-naphthyl acetate and α-naphthyl butyrate, were sensitive to organophosphates, and were classified as nonspecific aliesterases.

scholarly journals Opposite correlation of 25-hydroxy-vitamin D- and 1,25-dihydroxy-vitamin D-metabolites with gestational age, bone- and lipid-biomarkers in pregnant women

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Oleg Tsuprykov ◽  
Saban Elitok ◽  
Claudia Buse ◽  
Chang Chu ◽  
Bernhard Karl Krämer ◽  
...  
Keyword(s):  
Vitamin D ◽  
Alkaline Phosphatase ◽  
Pregnant Women ◽  
Clinical Chemistry ◽  
Water Soluble ◽  
Target Cells ◽  
Vitamin D Metabolites ◽  
Specific Alkaline Phosphatase ◽  
Bone Specific Alkaline Phosphatase ◽  
Group B

Abstract25-Hydroxyvitamin D (25OHD) and 1,25-dihydroxyvitamin D (1,25(OH)2D) need to be bound to carrier proteins to be transported to their target cells. The majority of either 25OHD or 1,25(OH)2D is bound to vitamin D-binding protein (DBP), a smaller fraction is bound to albumin and only very small amounts of 25OHD or 1,25(OH)2D are free. Albumin-bound 25OHD or 1,25(OH)2D is relatively easily available after dissociation from albumin. Thus, the sum of free and albumin-bound forms is called bioavailable 25OHD and bioavailable 1,25(OH)2D. Total 25OHD and 1,25(OH)2D are defined as the sum of free, albumin-bound and DBP-bound 25OHD and 1,25(OH)2D, respectively. This cross-sectional study in 427 pregnant women compared the correlation of the six vitamin D compounds with biomarkers of bone health, lipid metabolism, kidney function, endocrine parameters, and group B water-soluble vitamins. Among the 25OHD metabolites analysed, total 1,25(OH)2D showed clearly the best correlation with calcium, bone-specific alkaline phosphatase, adiponectin, LDL, HDL, urea, thyroxine, and group B water-soluble vitamins. When comparing the three 25OHD metabolites, both free 25OHD and bioavailable 25OHD showed overall good correlations with calcium, bone-specific alkaline phosphatase, adiponectin, LDL, HDL, urea, thyroxine, triiodothyronine, and group B water-soluble vitamins, The correlations of 1,25(OH)2D and 25OHD metabolites went always in opposite directions. Only PTH correlates always inversely with all six vitamin D compounds. In conclusion, free 25(OH)D and bioavailable 25(OH)D are more precise determinants of the vitamin D status than total 25(OH)D in normal pregnancy, whereas total 1,25(OH)2D is superior to free and bioavailable 1,25(OH)2D. Except for PTH, correlations of 25(OH)D and 1,25(OH)2D metabolites with typical clinical chemistry readouts go in opposite directions.

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