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 The introduction of the C-22–C-23 ethylenic linkage in ergosterol biosynthesis

1968 ◽  
Vol 106 (3) ◽  
pp. 623-626 ◽  
Author(s):  
M Akhtar ◽  
M. A. Parvez ◽  
P. F. Hunt
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Chemical Synthesis ◽  
Good Yield ◽  
The Other ◽  
Side Chain ◽  
Ergosterol Biosynthesis ◽  
Hydrogen Atoms ◽  
Whole Cells ◽  
C 23 ◽  
Methylene Derivative

Methods for the chemical synthesis of [23−3H2]lanosterol, [23,25−3H3]24-methyldihydrolanosterol and [24,28−3H2]24-methyldihydrolanosterol are described. It is shown that, in the biosynthesis of ergosterol from [26,27−14C2,23−3H2]lanosterol by the whole cells of Saccharomyces cerevisiae, one of the original C-23 hydrogen atoms is lost and the other is retained at C-23 of ergosterol. It is also shown that 24-methyldihydrolanosterol is converted into ergosterol in good yield and without prior conversion into a 24-methylene derivative. On the basis of these results possible pathways for the formation of the ergosterol side chain from a 24-methylene side chain are discussed.

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.

THE INFLUENCE OF SOME HEXITOLS AND SUGARS ON CO2 PRODUCTION BY STARVED AND X-IRRADIATED, STARVED YEAST CELLS

1967 ◽  
Vol 13 (7) ◽  
pp. 811-817 ◽  
Author(s):  
Edward Spoerl ◽  
R. J. Doyle
Keyword(s):  
High Capacity ◽  
The Other ◽  
Yeast Cells ◽  
Co2 Production ◽  
Stabilizing Agent ◽  
Other Hand ◽  
Radiation Induced ◽  
Lag Period ◽  
The Difference

The rates of CO2 production from glucose by irradiated and unirradiated yeast cells (incubated 21 hours in solutions of mannitol, ribose, methyl glucose, or cellobiose) were the same; but in a similar experiment, involving a 21-hour incubation in water, irradiated cells produced CO2 at a higher rate than did unirradiated cells. Incubation of the cells with the above compounds also eliminated a lag period in CO2 output and preserved a high capacity to produce CO2. On the other hand, incubation with glucose or fructose, though it eliminated the lag, lowered the rate of CO2 output and did not eliminate the difference in output between irradiated and unirradiated cells. Conversion of cells to spheroplasts also eliminated the radiation-induced difference in the rate of CO2 production, and, because sorbitol was used as a stabilizing agent for the spheroplasts, suggested first that sorbitol and other hexitols and sugars be examined. Reincubation, after a 21-hour starvation in water, with any of the compounds tested removed the lag period, though CO2 output was reduced.

Three Ways Aliphatic Aldehydes React with Nonstabilized Azomethine Ylides

Synlett ◽  
2020 ◽  
Vol 31 (04) ◽  
pp. 343-348
Author(s):  
Vladimir S. Moshkin ◽  
Evgeniya V. Gorbunova ◽  
Evgeny M. Buev ◽  
Vyacheslav Y. Sosnovskikh
Keyword(s):  
Mannich Bases ◽  
The Other ◽  
Azomethine Ylides ◽  
Similar Reaction ◽  
Hydrogen Atoms ◽  
Reaction Conditions ◽  
Aliphatic Aldehydes ◽  
Other Hand ◽  
Starting Compound ◽  
Alkyl Groups

Aliphatic aldehydes readily react with nonstabilized azomethine ylides in one of the three ways to give oxazolidines, pyrrolidines, or Mannich bases, depending on the structure of the starting compound and the reaction conditions. The use of N-(methoxymethyl)-N-[(trimethylsilyl)methyl]benzylamine in DMF provided 5-alkyloxazolidines in 40–97% yields. On the other hand, three-component reactions of aliphatic aldehydes bearing one α-hydrogen with N-methyl(benzyl)glycine and formaldehyde gives Mannich bases in yields of 47–98%. A similar reaction of aldehydes bearing branched alkyl groups and two hydrogen atoms at the α-position proceeds as a domino process that gives 3-alkyl-3-formylpyrrolidines in yields of 34–93%.

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.

Activity Comparison of MCM-41 and V-MCM-4 Catalysts for Ethanol Selective Oxidation and DRIFTS Analysis

2009 ◽  
Vol 7 (1) ◽  
Author(s):  
Yesim Gucbilmez ◽  
Timur Dogu ◽  
Suna Balci
Keyword(s):  
Hydrogen Atom ◽  
Gas Phase ◽  
Selective Oxidation ◽  
The Other ◽  
Lattice Oxygen ◽  
Molar Ratio ◽  
Surface Species ◽  
Other Hand ◽  
Activity Comparison ◽  
Mcm 41

The activity of a V-MCM-41 catalyst with a V/Si molar ratio of 0.04 was compared with the activity of a pure MCM-41 catalyst and some DRIFTS studies were performed in order to understand the mechanism of selective oxidation of ethanol. V-MCM-41 was found to be much more active than pure MCM-41, favouring the formation of high amounts of ethylene over 300°C. MCM-41, on the other hand, was found to favour the formation of acetaldehyde over ethylene at all studied temperatures. It was shown by reaction findings that over V-MCM-41, ethylene was produced mainly in the presence of gas phase oxygen whereas acetaldehyde was produced using the lattice oxygen even in the absence of gas phase oxygen. DRIFTS studies indicated the formation of acetaldehyde molecules from acetate-like surface species which were formed by the removal of a hydrogen atom from the ?-carbon of chemisorbed ethoxy species by the help of the lattice oxygen. On the other hand, removal of a hydrogen atom from the ?-carbon of the ethoxy species, in the presence of gas phase oxygen, resulted in the formation of vinyl-like surface species which then yielded ethylene molecules.

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.

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.

scholarly journals The biological conversion of 7-dehydrocholesterol into cholesterol and comments on the reduction of double bonds

1968 ◽  
Vol 106 (4) ◽  
pp. 803-810 ◽  
Author(s):  
D. C. Wilton ◽  
K A Munday ◽  
S. J. M. Skinner ◽  
M Akhtar
Keyword(s):  
Hydrogen Atom ◽  
Rat Liver ◽  
Enzyme System ◽  
Tritiated Water ◽  
Liver Homogenate ◽  
Double Bonds ◽  
Hydrogen Atoms ◽  
Biological Conversion ◽  
Microsomal Pellet

It is shown that the 7-dehydrocholesterol reductase-catalysed conversion of 7-dehydrocholesterol into cholesterol (II), with a 105000g microsomal pellet of rat liver in the presence of [4−3H2]NADPH, results in the transfer of radioactivity to the 7α-position of cholesterol. When the conversion is carried out in the presence of tritiated water the label is introduced exclusively at the 8β-position. However, when the conversion of 7-dehydrocholesterol into cholesterol is performed with a 500g supernatant of rat liver homogenate the radioactivity is incorporated at both the 7α- and the 8β-position. Evidence is provided for the presence of an enzyme system in the 500g supernatant that catalyses an equilibration of hydrogen atoms between those at the 4-position of NADPH and those of water. The work with stereospecifically labelled cofactors shows that both the equilibrating system and the 7-dehydrocholesterol reductase utilize the 4B-hydrogen atom of NADPH. In the light of these results a mechanism for the reduction of carbon–carbon double bonds is discussed.

scholarly journals The stereospecificity of the reduction of nitrate by reduced nicotinamide-adenine dinucleotides catalysed by Candida utilis preparations

1982 ◽  
Vol 205 (3) ◽  
pp. 581-584 ◽  
Author(s):  
D D Davies ◽  
P Kenworthy
Keyword(s):  
Hydrogen Atom ◽  
Nitrate Reductase ◽  
Isotope Effect ◽  
Candida Utilis ◽  
Kinetic Isotope Effect ◽  
The Other ◽  
Nicotinamide Adenine ◽  
Hydrogen Atoms ◽  
Kinetic Isotope ◽  
High Degree

The reduction of nitrate by reduced nicotinamide-adenine dinucleotides, catalysed by extract of Candida utilis, exhibits an apparent high degree of stereospecificity for the ‘B’ methylene hydrogen atom of NADPH and mixed stereospecificity for the methylene hydrogen atoms of NADH. Purified nitrate reductase, on the other hand, exhibits ‘A’ stereospecificity for NADH and NADPH. The apparent switch of stereospecificity from the ‘B’ to the ‘A’ side of NADPH, which occurs after purification of the enzyme, is partly explained by the fact that in crude extracts nitrate is reduced completely to ammonia. Nitrite does not accumulate but is reduced to ammonia by nitrite dehydrogenase, which is ‘B’-specific, so that up to 75% of hydrogen removed from NADPH during the reduction of nitrate could occur from the ‘B’ side. A further increase in the removal of hydrogen from the ‘B’ side of NADPH could be the kinetic isotope effect that is observed when [‘A’-3H]NADPH is the reductant, the H-C bond being cleaved 2.3 times faster than the 3H-C bond. The mixed stereospecificity observed with NADH has been traced to an uncharacterized enzyme that catalyses a ‘B’-specific exchange between NAD+ and NADH. This reaction is discussed in relation to the possibility that it may explain other cases of apparent mixed stereospecificity that have been reported.

Sign in / Sign up

Export Citation Format

Share Document