scholarly journals STABLE SUDANOPHILIA OF HUMAN NEUTROPHIL LEUCOCYTES IN RELATION TO PEROXIDASE AND OXIDASE

10.1177/1.1.8 ◽  
1953 ◽  
Vol 1 (1) ◽  
pp. 8-26 ◽  
Author(s):  
R. D. LILLIE ◽  
H. J. BURTNER
Keyword(s):  
Hydrogen Peroxide ◽  
Fatty Acid ◽  
Human Neutrophil ◽  
Polymorphonuclear Leucocytes ◽  
Potassium Bichromate ◽  
Sudan Dyes ◽  
Variable Size ◽  
Chemical Combination ◽  
Sudan Dye ◽  
Fatty Acid Peroxide

It seems improbable that leucocyte oxidase is a fatty acid peroxide, as suggested by Sehrt, on these grounds: 1. Positive reactions for aldehyde and for ethylene groups are not obtained. Hence the presence of fatty acid peroxides in leucocytes seems unlikely. 2. Peroxidase has been isolated from leucocytes by Agner. Histochemical behavior on treatment with adverse reagents and with heat indicates similarity of benzidine peroxidase and of indophenol oxidase, but dissimilarity of these from the sudanophil substance in leucocytes. 3. Sudan dyes demonstrate or produce in neutrophil leucocytes deeply colored granules of quite variable size, and the size of the granules apparently increases with the duration of staining. 4. The demonstration of sudanophil granules in leucocytes is accomplished with difficulty. The colored granules are highly stable toward many Sudan dye solvents. Decolorization is difficult and recoloration is uncertain. 5. True fats and lipoids, after staining with Sudan dyes, are readily decolorized by appropriate dye solvents and are restainable in apparently undiminished amounts. 6. Some oxidants tend to impair sudanophilia of leucocytes. Potassium bichromate improves the preservation of sudanophil lipoids, as in the Ciaccio method, but destroys the sudanophilia of polymorphonuclear leucocytes. 7. Hydrogen peroxide apparently possesses an inconstant and irregular, though sometimes quite pronounced, accelerating effect on the production of Sudan stained granules in leucocytes. 8. The sudanophilia of leucocytes depends on an as yet unexplained chemical combination of the dyes with cytoplasmic constituents which are probably not in the form of preexisting granules, rather than on lipoid staining.

scholarly journals Activation of endothelial cell phospholipase D by hydrogen peroxide and fatty acid hydroperoxide.

1993 ◽  
Vol 268 (2) ◽  
pp. 930-937
Author(s):  
V. Natarajan ◽  
M.M. Taher ◽  
B. Roehm ◽  
N.L. Parinandi ◽  
H.H. Schmid ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Fatty Acid ◽  
Endothelial Cell ◽  
Phospholipase D ◽  
Fatty Acid Hydroperoxide ◽  
Acid Hydroperoxide

scholarly journals The Study Of Conversion Cpo To Polyol (Polyalcohol)

REAKTOR ◽  
2017 ◽  
Vol 11 (1) ◽  
pp. 8
Author(s):  
F. S. Budi ◽  
Z. Abidin
Keyword(s):  
Hydrogen Peroxide ◽  
Fatty Acid ◽  
Optimum Condition ◽  
Formic Acid ◽  
The Other ◽  
Hydroxyl Number ◽  
Main Component

Indonesia is the second big CPO producer after Malaysia. The CPO production of Indonesia gradually increases and reaches 8.2 million tones. About two third of it is used to meet the domestic will receive little income. Therefore, it must be converted into the other product, which has the high value. The main component of it is glyceride composed of glycerol  and fatty acid. The glyceride can be converted into polyol (polyalcohol) which is the material in manufacturing polyurethane, cosmetic, lubricant etc. the process of converting of CPO into polyol is called  the hydroxylation. This research aim to study the hydroxylation process of CPO into polyol and to optimize the variable which really affect the hydroxyl number of product. Based on the experiment, the optimum condition of hydroxylation of CPO with the hydrogen peroxide (H2O2) and the formic acid (HCOOH) into polyol is got as follows: temperature 50 0C, composition of reactan 40% and time 2 hours. The polyol produced has the hydroxyl number 148.Keywords : CPO, hydroxylation, polyol

Protection against Superoxide and Hydrogen Peroxide in Synovial Fluid from Rheumatoid Patients

1981 ◽  
Vol 61 (4) ◽  
pp. 483-486 ◽  
Author(s):  
D. R. Blake ◽  
N. D. Hall ◽  
D. A. Treby ◽  
B. Halliwell ◽  
J. M. C. Gutteridge
Keyword(s):  
Hydrogen Peroxide ◽  
Synovial Fluid ◽  
Oxygen Radicals ◽  
Superoxide Radical ◽  
Joint Disease ◽  
Polymorphonuclear Leucocytes ◽  
Inflammatory Joint Disease ◽  
Normal Range ◽  
Lubricating Properties

1. On exposure of synovial fluid to superoxide and hydrogen peroxide, generated enzymically or by activated polymorphonuclear leucocytes, hyaluronic acid is depolymerized and the fluid loses its lubricating properties. The ability of synovial fluid from rheumatoid patients to scavenge superoxide and hydrogen peroxide was therefore examined. 2. Synovial fluid from a range of rheumatoid patients contained no superoxide dismutase activity, insufficient caeruloplasmin to scavenge any superoxide radical and little, if any, catalase activity. 3. Total ascorbate (reduced ascorbate + dehydroascorbate) concentrations in the plasma and synovial fluid of rheumatoid patients were similar in each case. The values are at the low end of the normal range. 4. These results are discussed in relation to the role of oxygen radicals in inflammatory joint disease.

scholarly journals Sites of superoxide and hydrogen peroxide production during fatty acid oxidation in rat skeletal muscle mitochondria

2013 ◽  
Vol 61 ◽  
pp. 298-309 ◽  
Author(s):  
Irina V. Perevoshchikova ◽  
Casey L. Quinlan ◽  
Adam L. Orr ◽  
Akos A. Gerencser ◽  
Martin D. Brand
Keyword(s):  
Skeletal Muscle ◽  
Hydrogen Peroxide ◽  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Acid Oxidation ◽  
Rat Skeletal Muscle ◽  
Hydrogen Peroxide Production ◽  
Muscle Mitochondria ◽  
Skeletal Muscle Mitochondria

scholarly journals Inhibition of Human Neutrophil IL-8 Production by Hydrogen Peroxide and Dysregulation in Chronic Granulomatous Disease

2004 ◽  
Vol 174 (1) ◽  
pp. 411-417 ◽  
Author(s):  
Julie A. Lekstrom-Himes ◽  
Douglas B. Kuhns ◽  
W. Gregory Alvord ◽  
John I. Gallin
Keyword(s):  
Hydrogen Peroxide ◽  
Chronic Granulomatous Disease ◽  
Human Neutrophil ◽  
Granulomatous Disease

Oxidation-resistant variants of recombinant anti-leucoprotease are better inhibitors of human-neutrophil-elastase-induced emphysema in hamsters than natural recombinant antileucoprotease

1991 ◽  
Vol 81 (6) ◽  
pp. 777-784 ◽  
Author(s):  
A. Rudolphus ◽  
R. Heinzel-Wieland ◽  
V. A. M. M. Vincent ◽  
D. Saunders ◽  
G. J. Steffens ◽  
...  
Keyword(s):  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Site Directed Mutagenesis ◽  
Human Neutrophil Elastase ◽  
Polymorphonuclear Leucocytes ◽  
Inhibitory Effects ◽  
Oxidative Inactivation ◽  
Methionine Residues

1. Antileucoprotease, being sensitive to oxidative inactivation, can be produced by recombinant techniques. Via site-directed mutagenesis, two mutants of recombinant antileucoprotease were produced in which one or more of the oxidation-sensitive methionine residues were replaced by leucine: in rALP242, methionine-73 was replaced by leucine, and in rALP231, leucine was substituted for four methionine residues. In vitro, native antileucoprotease and the recombinant antileucoprotease preparations have similar inhibitory characteristics towards human neutrophil elastase. We hypothesized that replacement of methionine residues in the antileucoprotease molecule would result in a reduced oxidation sensitivity of the mutants. 2. After incubation of recombinant antileucoprotease and its mutants with increasing dosages of cis-platinum(II)diammine dichloride, we observed that native antileucoprotease and recombinant antileucoprotease were inactivated by this reagent to the same extent. Compared with this, rALP242 was less inactivated, whereas the inhibitory capacity of rALP231 was not influenced by cis-platinum(II)diammine dichloride at all. 3. After incubation of recombinant antileucoprotease, rALP242 and rALP231 with triggered polymorphonuclear leucocytes, which are thought to produce an excess of oxidants, we measured residual inhibitory activities towards human neutrophil elastase of 10%, 55% and 87%, respectively. 4. In vivo, the inhibitory effects of intratracheally administered rALP242 and rALP231 towards human-neutrophil-elastase-induced emphysema were significantly greater than that of recombinant antileucoprotease. There were no significant differences between the mutants. With respect to secretory cell metaplasia and haemorrhage, rALP231 tended to be a better inhibitor than recombinant antileucoprotease and rALP242. 5. We conclude that the recombinant antileucoprotease mutants are less sensitive to oxidation and consequently inhibit human-neutrophil-elastase-induced emphysema to a greater extent than recombinant antileucoprotease.

scholarly journals THE NATURE OF SERUM ANTITRYPSIN

1914 ◽  
Vol 19 (5) ◽  
pp. 459-479 ◽  
Author(s):  
James W. Jobling ◽  
William Petersen
Keyword(s):  
Hydrogen Peroxide ◽  
Fatty Acids ◽  
Fatty Acid ◽  
Potassium Iodide ◽  
Unsaturated Fatty Acids ◽  
Serum Lipase ◽  
Enzyme Action ◽  
Inhibiting Action

1. The ferment-inhibiting action of the serum is due to the presence of compounds of the unsaturated fatty acids. 2. These fatty acid compounds may be removed from the serum by means of chloroform or ether. 3. Soaps prepared by saponifying the chloroform or ether extracts inhibit the action of trypsin. 4. The anti-enzyme action of the serum can be removed by filtering acid serum through kaolin, and can in part be restored by extracting the kaolin. 5. The decrease in strength of anti-enzyme in old sera is probably due to the action of the serum lipase. 6. Iodin, potassium iodide, or hydrogen peroxide remove the inhibiting action of the serum. 7. Soaps of the unsaturated fatty acids lose their ferment-inhibiting action when heated with serum at 70° C.

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