BIOGENESE VON ÖSTRIOL-3-MONOGLUCURONID

1967 ◽  
Vol 56 (3) ◽  
pp. 403-412 ◽  
Author(s):  
K. Dahm ◽  
Monika Lindlau ◽  
H. Breuer
Keyword(s):  
Rat Liver ◽  
Steric Hindrance ◽  
Microsomal Fraction ◽  
Enzyme System ◽  
The Other ◽  
Human Intestine ◽  
Enzyme Preparations ◽  
Other Hand ◽  
Enzymatic Reduction

ABSTRACT The biogenesis of oestriol 3-monoglucuronide has been studied using different enzyme preparations of human intestine and placenta as well as of rat liver. After incubation of oestriol with the microsomal fraction of human intestine, oestriol 3-monoglucuronide was found in addition to oestriol 16α-monoglucuronide and oestriol 17β-monoglucuronide. No oestriol 3-monoglucuronide was found when 16α-hydroxyoestrone 3-monoglucuronide, prepared biosynthetically, was incubated with a 24-fold purified human placental 17β-hydroxysteroid:NAD-oxidoreductase. On the other hand, no oestriol 3-monoglucuronide was formed when 17β-oestradiol 3-monoglucuronide was subjected to the action of the microsomal 16α-hydroxylase of rat liver. These results may be explained by steric hindrance of the enzyme system involved. On the basis of the present findings it can be concluded that oestriol 3-monoglucuronide arises exclusively by direct glucuronidation of oestriol, and not by enzymatic reduction of 16α-hydroxyoestrone 3-monoglucuronide or by 16α-hydroxylation of 17β-oestradiol 3-monoglucuronide.

BIOGENESE VON ÖSTRIOL-16α-MONOGLUCURONID UND ÖSTRIOL-17β-MONOGLUCURONID

1966 ◽  
Vol 52 (1) ◽  
pp. 43-53 ◽  
Author(s):  
K. Dahm ◽  
H. Breuer
Keyword(s):  
Rat Liver ◽  
Steric Hindrance ◽  
Microsomal Fraction ◽  
Enzyme System ◽  
The Other ◽  
Human Intestine ◽  
Main Metabolite ◽  
Enzyme Preparations ◽  
Glucuronyl Transferase ◽  
Enzymatic Reduction

ABSTRACT The biogenesis of oestriol 16α-monoglucuronide and oestriol 17β-monoglucuronide has been studied using different enzyme preparations of human intestine, placenta and liver as well as of rat liver. After incubation of oestriol with the microsomal fraction of human intestine or rat liver, oestriol 16α-monoglucuronide was found as main metabolite, whereas oestriol 17β-monoglucuronide was formed in smaller amounts. When the 100 000 × g supernatant of human intestine was precipitated with ammonium sulphate (30–60% saturation), a glucuronyl transferase was obtained which catalysed the formation of oestriol 17β-monoglucuronide only. No oestriol 16α-monoglucuronide was found when 16α-hydroxyoestrone 16α-monoglucuronide was incubated with either the cytoplasmic 17β-hydroxysteroid:NAD(P)-oxidoreductase of human intestine and rat liver or with a 37-fold purified human placental 17β-hydroxysteroid:NAD-oxidoreductase. On the other hand, no oestriol 17β-monoglucuronide was formed when 17β-oestradiol 17β-monoglucuronide was subjected to the action of the microsomal 16α-hydroxylase of rat liver. These results may be explained by steric hindrance of the enzyme system involved. On the basis of the present findings it can be concluded that oestriol 16α-monoglucuronide arises exclusively by direct glucuronidation of oestriol, and not by enzymatic reduction of 16α-hydroxyoestrone 16α-monoglucuronide. Similarly, oestriol 17β-monoglucuronide is most probably formed only by direct glucuronidation of oestriol, and not by 16α-hydroxylation of 17β-oestradiol 17β-monoglucuronide.

Conversion of Flavanone to Flavone, Dihydroflavonol and Flavonol with an Enzyme System from Cell Cultures of Parsley

1981 ◽  
Vol 36 (9-10) ◽  
pp. 742-750 ◽  
Author(s):  
L. Britsch ◽  
W. Heller ◽  
H. Grisebach
Keyword(s):  
Microsomal Fraction ◽  
Specific Activity ◽  
Enzyme System ◽  
High Specific Activity ◽  
Cell Suspension Cultures ◽  
Soluble Enzyme ◽  
Enzyme Preparations ◽  
Malonyl Coa ◽  
In Vitro Biosynthesis

Abstract Soluble enzyme preparations from irradiated cell suspension cultures of parsley (Petroselinum hortense Hoffm.) catalyse the conversion of flavanone to flavone, dihydroflavonol and flavonol. These reactions require 2-oxoglutarate, Fe2+ and ascorbate as cofactors. In the presence of these cofactors conversion of dihydroflavonol to flavonol was also observed. With this system in vitro biosynthesis of radioactive flavone, dihydroflavonol and flavonol from [2-14C]malonyl-CoA and 4-coumaroyl-CoA in good yield and with high specific activity is possible.We postulate that synthesis of flavone and flavonol from flavanone proceeds via 2-hydroxy-and 2,3-dihydroxyflavanone, respectively, with subsequent dehydration.The microsomal fraction of the parsley cells contains an NADPH-dependent flavanone 3'-hydroxylase.

scholarly journals Effects of di-isopropyl phosphorofluoridate on rat liver microsomal and lysosomal β-glucuronidase

1977 ◽  
Vol 164 (3) ◽  
pp. 549-556 ◽  
Author(s):  
Brian Mandell ◽  
Philip Stahl
Keyword(s):  
Rat Liver ◽  
Early Time ◽  
Subcellular Fractionation ◽  
Isolated Hepatocytes ◽  
The Other ◽  
Time Points ◽  
Glucuronidase Activity ◽  
Other Hand ◽  
Microsomal Membranes

iPr2P-F (di-isopropyl phosphorofluoridate) administration to rats produces a liver-dependent specific elevation of plasma β-glucuronidase activity. The response is unaffected by puromycin pretreatment. By using subcellular-fractionation techniques, the rise in plasma β-glucuronidase activity was correlated temporally with a fall in liver microsomal β-glucuronidase activity. After iPr2P-F treatment, liver microsomal membranes are depleted of β-glucuronidase but slowly return to normal over 1 week. On the other hand, liver lysosomal β-glucuronidase activity is high at early time points (less than 60min) after iPr2P-F administration but decreases to below control values; this lasts for a few days. The response to iPr2P-F was demonstrated in isolated hepatocytes prepared from iPr2P-F-treated rats. In such preparations, microsomal β-glucuronidase is lost rapidly, followed by a specific decrease in hepatocyte lysosomal β-glucuronidase. The results suggest that a pool of microsomal β-glucuronidase serves as precursor to plasma β-glucuronidase in iPr2P-F-treated rats, and further, that microsomal β-glucuronidase may serve as precursor to lysosomal β-glucuronidase.

FURTHER OBSERVATIONS ON THE ENZYMATIC REDUCTION OF TETRAZOLIUM SALTS BY MONOAMINES

1958 ◽  
Vol 36 (6) ◽  
pp. 587-594 ◽  
Author(s):  
J. R. Lagnado ◽  
T. L. Sourkes
Keyword(s):  
Rat Liver ◽  
Metal Binding ◽  
Enzyme System ◽  
Enzymatic Reaction ◽  
Free Base ◽  
Tetrazolium Salts ◽  
Enzymatic Reduction ◽  
Tissue Homogenates ◽  
Cofactor Activity

Studies on the role of purines as cofactors in the enzymatic reduction of tetrazolium salts by monoamines have led to the following results: (1) With whole rat liver extracts as the source of enzymes, several purines exhibit cofactor activity either as the free base or as the corresponding riboside and ribotide derivatives. (2) In contrast to this, mitochondrial material from rat liver is active only if adenylic acid or one of several ribotidic derivatives containing an adenylyl or similar moiety is used as cofactor. (3) Mitochondrial material utilizes hypoxanthine as cofactor for the amine/tetrazolium system only in combination with the supernatant obtained by centrifugation of tissue homogenates at 20,000 g. The additional factor present in this supernatant portion is heat-labile and nondialyzable. The possibility that this additional factor is an enzyme or enzymes converting the free base to the ribotide is discussed.Inhibition studies have revealed that the amine/tetrazolium enzyme system is sensitive to several metal-binding agents, but no direct evidence for the role of a metal in the enzymatic reaction could be obtained. It was also found that nicotinamide and adenine, neither of which exhibits cofactor activity, are potent inhibitors of the enzyme system studied.

scholarly journals The stereochemistry of hydrogen elimination from C-7 in cholesterol and ergosterol biosynthesis

1970 ◽  
Vol 117 (3) ◽  
pp. 539-542 ◽  
Author(s):  
M. Akhtar ◽  
A. D. Rahimtula ◽  
D. C. Wilton
Keyword(s):  
Hydrogen Atom ◽  
Rat Liver ◽  
The Other ◽  
Yeast Cells ◽  
Ergosterol Biosynthesis ◽  
Hydrogen Atoms ◽  
Hydrogen Elimination ◽  
Other Hand

The synthesis of [7α-3H]lanosterol is described. It is shown that in the conversion of [7α-3H,26,27-14C2]lanosterol into cholesterol by a rat liver system, it is the 7β-hydrogen atom that is predominantly removed. On the other hand, the conversion of doubly labelled lanosterol into ergosterol by whole yeast cells results in the loss of the 7α-hydrogen atom. These results therefore suggest that the C-7 hydrogen atoms with opposite stereochemistry are labilized by the rat liver and the yeast Δ8–Δ7 steroid isomerases.

scholarly journals Identity of purified monoacylglycerol lipase, palmitoyl-CoA hydrolase and aspirin-metabolizing carboxylesterase from rat liver microsomal fractions. A comparative study with enzymes purified in different laboratories

1985 ◽  
Vol 232 (2) ◽  
pp. 479-483 ◽  
Author(s):  
R Mentlein ◽  
R K Berge ◽  
E Heymann
Keyword(s):  
Rat Liver ◽  
Microsomal Fraction ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Monoacylglycerol Lipase ◽  
Enzyme Preparations ◽  
Nitrophenyl Phosphate ◽  
Liver Microsomal Fraction ◽  
Coa Hydrolase ◽  
Rat Liver Cytosol

Two purified carboxylesterases that were isolated from a rat liver microsomal fraction in a Norwegian and a German laboratory were compared. The Norwegian enzyme preparation was classified as palmitoyl-CoA hydrolase (EC 3.1.2.2) in many earlier papers, whereas the German preparation was termed monoacylglycerol lipase (EC 3.1.1.23) or esterase pI 6.2/6.4 (non-specific carboxylesterase, EC 3.1.1.1). Antisera against the two purified enzyme preparations were cross-reactive. The two proteins co-migrate in sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Both enzymes exhibit identical inhibition characteristics with Mg2+, Ca2+ and bis-(4-nitrophenyl) phosphate if assayed with the two substrates palmitoyl-CoA and phenyl butyrate. It is concluded that the two esterase preparations are identical. However, immunoprecipitation and inhibition experiments confirm that this microsomal lipase differs from the palmitoyl-CoA hydrolases of rat liver cytosol and mitochondria.

Lipogenesis from ketone bodies in the perfused rat liver: effects of acetate and ethanol

1987 ◽  
Vol 65 (11) ◽  
pp. 989-996 ◽  
Author(s):  
Gerda Endemann ◽  
Patrick G. Goetz ◽  
John F. Tomera ◽  
William M. Rand ◽  
Sylvain Desrochers ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Rat Liver ◽  
Ketone Body ◽  
Ketone Bodies ◽  
The Other ◽  
Ethanol Metabolism ◽  
Perfused Rat Liver ◽  
Other Hand

The interactions between acetate or ethanol metabolism, lipogenesis, and ketone body utilization have been studied in isolated livers from fed rats perfused with 15 mM glucose and 10 mM acetate or ethanol. The contribution of acetate to ketogenesis is constant; on the other hand, the contribution of ethanol to ketogenesis increases with time, presumably because of the accumulation of acetate in the perfusate. Ketogenesis is decreased in the presence of ethanol (but not acetate), while ketone body utilization is not affected by ethanol or acetate. Acetate contributes one third and ethanol contributes one half of the carbon incorporated into fatty acids and 3-β-hydroxysterols. Only a small fraction (less than 5%) of the incorporation of acetate or ethanol into fatty acids and sterols occurs via transient incorporation into ketone bodies.

scholarly journals Effect of stirring during fixation upon immunofluorescence. Results with distribution of albumin-producing cells in liver.

1976 ◽  
Vol 24 (8) ◽  
pp. 926-932 ◽  
Author(s):  
M Horikawa ◽  
N Chisaka ◽  
S Yokoyama ◽  
T Onoé
Keyword(s):  
Rat Liver ◽  
The Other ◽  
Magnetic Stirrer ◽  
Other Hand ◽  
Rapid Fixation ◽  
Protein Free Diet

When the immunofluroscent study on the distribution and the incidence of albumin-producing hepatocytes in the rat liver was performed by the method of Sainte-Marie, the number of positive cells showed various values (10-60%). It was surmised that when the permeability of the fixative was delayed, albumin had flowed out from the cytoplasm of the unfixed hepatocytes. By the simple means of constant stirring of the fixative using a magnetic stirrer, we accomplished rapid fixation and achieved results in which positive cells attained 100%. On the other hand, the incidence of positive cells decreased markedly when rats were fed a protein-free diet.

FURTHER OBSERVATIONS ON THE ENZYMATIC REDUCTION OF TETRAZOLIUM SALTS BY MONOAMINES

1958 ◽  
Vol 36 (1) ◽  
pp. 587-594 ◽  
Author(s):  
J. R. Lagnado ◽  
T. L. Sourkes
Keyword(s):  
Rat Liver ◽  
Metal Binding ◽  
Enzyme System ◽  
Enzymatic Reaction ◽  
Free Base ◽  
Tetrazolium Salts ◽  
Enzymatic Reduction ◽  
Tissue Homogenates ◽  
Cofactor Activity

Studies on the role of purines as cofactors in the enzymatic reduction of tetrazolium salts by monoamines have led to the following results: (1) With whole rat liver extracts as the source of enzymes, several purines exhibit cofactor activity either as the free base or as the corresponding riboside and ribotide derivatives. (2) In contrast to this, mitochondrial material from rat liver is active only if adenylic acid or one of several ribotidic derivatives containing an adenylyl or similar moiety is used as cofactor. (3) Mitochondrial material utilizes hypoxanthine as cofactor for the amine/tetrazolium system only in combination with the supernatant obtained by centrifugation of tissue homogenates at 20,000 g. The additional factor present in this supernatant portion is heat-labile and nondialyzable. The possibility that this additional factor is an enzyme or enzymes converting the free base to the ribotide is discussed.Inhibition studies have revealed that the amine/tetrazolium enzyme system is sensitive to several metal-binding agents, but no direct evidence for the role of a metal in the enzymatic reaction could be obtained. It was also found that nicotinamide and adenine, neither of which exhibits cofactor activity, are potent inhibitors of the enzyme system studied.

Effect of 5′-Terminated (2′— 5′)-01igoadenylates on Cap Degrading Activities in Rat Liver Nuclei

1983 ◽  
Vol 38 (7-8) ◽  
pp. 631-634 ◽  
Author(s):  
Winfried Michels ◽  
Eckhard Schlimme
Keyword(s):  
Synergistic Effect ◽  
Rat Liver ◽  
Cellular Metabolism ◽  
The Other ◽  
Rat Liver Nuclei ◽  
Other Hand ◽  
Infected Cells ◽  
Liver Nuclei ◽  
Exonucleolytic Degradation

(2'-5')-oligoadenylates bearing a 5'-terminal triphosphate or a 5'GTP-group inhibit the activity of a dinucleoside triphosphatase in rat liver nuclei thereby protecting mRNA against 5'-exonucleolytic degradation. (2'-5')-oligoadenylates, on the other hand, were known to enhance the activity of an endoribonuclease, RNaseF. Thus a synergistic effect may be assumed in vivo, i.e. cellular metabolism seems to be protected twice in virus-infected cells.

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