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.

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 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.

scholarly journals The 3-methylhistidine content of human tissues

1979 ◽  
Vol 42 (3) ◽  
pp. 567-570 ◽  
Author(s):  
M. Elia ◽  
A. Carter ◽  
R. Smith
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Dry Weight ◽  
Human Tissues ◽  
Post Mortem ◽  
Striated Muscles ◽  
Significant Difference ◽  
Use Values ◽  
Liver And Kidney ◽  
The Mean

1. The amount of 3-methylhistidine (3-MeH) has been measured in eighty-eight samples of tissue taken Post-mortem from five adults.2. The highest concentration (μmol/g fat-free dry weight) of 3-MeH was in skeletal muscle (3.31 ± 0.05); intermediate values (2–3) were found in cardiac muscle and those tissues containing smooth muscle; and low values (less than I) occurred in parenchymal tissues such as liver and kidney.3. There was little variation between the mean 3-MeH content of striated muscles in different individuals, and no significant difference between the 3-MeH concentrations of striated muscles taken from six different sites.4. The results suggest that it is justifiable to use values obtained from single muscles to calculate the rate of myofibrillar breakdown from urinary 3-MeH excretion.

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.

ACTION OF ORGANOPHOSPHORUS COMPOUNDS UPON ESTERASES OF HUMAN LIVER

1963 ◽  
Vol 41 (1) ◽  
pp. 1537-1546 ◽  
Author(s):  
D. J. Ecobichon ◽  
W. Kalow
Keyword(s):  
Human Serum ◽  
Human Liver ◽  
Organophosphorus Compounds ◽  
Chemical Conversion ◽  
The Other ◽  
Serum Cholinesterase ◽  
Organophosphorus Insecticides ◽  
Low Concentrations ◽  
Starch Gel ◽  
Per Se

Human serum and liver esterases separated electrophoretically in starch gel were exposed to two series of organophosphorus insecticides. One series consisted of compounds active per se, the other of analogues requiring metabolic or chemical conversion to produce potent anticholinesterases. The results indicated that only one fraction of the liver, designated as zone L-2, is inhibited by low concentrations of all insecticides. This fraction shows a similar pattern of susceptibility to different inhibitors as does human serum cholinesterase. Of the other two zones of activity in liver, zone L-1 was found to be more susceptible to activated thionate, dithioate, and thioether derivatives than was zone L-3, while the latter zone was more susceptible to phosphates active per se.

ACTION OF ORGANOPHOSPHORUS COMPOUNDS UPON ESTERASES OF HUMAN LIVER

1963 ◽  
Vol 41 (7) ◽  
pp. 1537-1546 ◽  
Author(s):  
D. J. Ecobichon ◽  
W. Kalow
Keyword(s):  
Human Serum ◽  
Human Liver ◽  
Organophosphorus Compounds ◽  
Chemical Conversion ◽  
The Other ◽  
Serum Cholinesterase ◽  
Organophosphorus Insecticides ◽  
Low Concentrations ◽  
Starch Gel ◽  
Per Se

Human serum and liver esterases separated electrophoretically in starch gel were exposed to two series of organophosphorus insecticides. One series consisted of compounds active per se, the other of analogues requiring metabolic or chemical conversion to produce potent anticholinesterases. The results indicated that only one fraction of the liver, designated as zone L-2, is inhibited by low concentrations of all insecticides. This fraction shows a similar pattern of susceptibility to different inhibitors as does human serum cholinesterase. Of the other two zones of activity in liver, zone L-1 was found to be more susceptible to activated thionate, dithioate, and thioether derivatives than was zone L-3, while the latter zone was more susceptible to phosphates active per se.

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.

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.

Electron Probe Analysis of Muscle

1982 ◽  
Vol 40 ◽  
pp. 398-401
Author(s):  
A. V. Somlyo ◽  
H. Shuman ◽  
A. P. Somlyo
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Sarcoplasmic Reticulum ◽  
Resting State ◽  
Binding Sites ◽  
Electron Probe ◽  
Frog Skeletal Muscle ◽  
Electron Probe Analysis ◽  
Probe Analysis

Electron probe analysis of frozen dried cryosections of frog skeletal muscle, rabbit vascular smooth muscle and of isolated, hyperpermeab1 e rabbit cardiac myocytes has been used to determine the composition of the cytoplasm and organelles in the resting state as well as during contraction. The concentration of elements within the organelles reflects the permeabilities of the organelle membranes to the cytoplasmic ions as well as binding sites. The measurements of [Ca] in the sarcoplasmic reticulum (SR) and mitochondria at rest and during contraction, have direct bearing on their role as release and/or storage sites for Ca in situ.

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