scholarly journals EFFECTS OF TRITON X-100 UPON THE ACTIVITY OF SOME ELECTROPHORETICALLY SEPARATED ACID PHOSPHATASES AND ESTERASES

1965 ◽  
Vol 13 (6) ◽  
pp. 434-440 ◽  
Author(s):  
SALLY LYMAN ALLEN ◽  
JOHN M. ALLEN ◽  
BARBARA MORRISON LICHT
Keyword(s):  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Rat Liver ◽  
Tetrahymena Pyriformis ◽  
Fatty Acid Esters ◽  
Acid Phosphatases ◽  
Ionic Detergent ◽  
Starch Gels ◽  
Triton X ◽  
Acid Esters

Triton X-100, a non-ionic detergent, was incorporated into reaction mixtures used for the visualization of esterases and acid phosphatases separated by electrophoresis in starch gels. Its effects were tested, in combination with 12 different substrates, on enzymes derived from Tetrahymena pyriformis and rat liver. The effects of Triton X-100 were complex. It promoted the solubilization of some substrates, notably the α-naphthyl fatty acid esters. It also altered the color of the enzymatically produced end product. The net effect was apparent enhancement of enzymatic activity with certain substrates and apparent inhibition of enzymatic activity with other substrates. Differential activation and inhibition of some of the electrophoretically resolved enzymes was observed. Both quantitative and electrophoretic studies indicated that Triton X-100 is an activator of certain esterases. A cathodally migrating acid phosphatase of rat liver was activated by Triton X-100 in the presence of naphthol AS, naphthol AS-BI, or naphthol AS-MX phosphates.

Comparison of the Thermostability Properties of Three Acid Phosphatases from Molds: Aspergillus fumigatusPhytase, A. niger Phytase, and A. nigerpH 2.5 Acid Phosphatase

1998 ◽  
Vol 64 (11) ◽  
pp. 4446-4451 ◽  
Author(s):  
Markus Wyss ◽  
Luis Pasamontes ◽  
Roland Rémy ◽  
Josiane Kohler ◽  
Eric Kusznir ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Aspergillus Niger ◽  
Enzymatic Activity ◽  
Conformational Changes ◽  
Animal Feed ◽  
Heat Denaturation ◽  
Acid Phosphatases ◽  
Active Conformation ◽  
Feed Supplements ◽  
Optimum Ph

ABSTRACT Enzymes that are used as animal feed supplements should be able to withstand temperatures of 60 to 90°C, which may be reached during the feed pelleting process. The thermostability properties of three histidine acid phosphatases, Aspergillus fumigatus phytase,Aspergillus niger phytase, and A. niger optimum pH 2.5 acid phosphatase, were investigated by measuring circular dichroism, fluorescence, and enzymatic activity. The phytases ofA. fumigatus and A. niger were both denatured at temperatures between 50 and 70°C. After heat denaturation at temperatures up to 90°C, A. fumigatus phytase refolded completely into a nativelike, fully active conformation, while in the case of A. niger phytase exposure to 55 to 90°C was associated with an irreversible conformational change and with losses in enzymatic activity of 70 to 80%. In contrast to these two phytases,A. niger pH 2.5 acid phosphatase displayed considerably higher thermostability; denaturation, conformational changes, and irreversible inactivation were observed only at temperatures of ≥80°C. In feed pelleting experiments performed at 75°C, the recoveries of the enzymatic activities of the three acid phosphatases were similar (63 to 73%). At 85°C, however, the recovery of enzymatic activity was considerably higher for A. fumigatusphytase (51%) than for A. niger phytase (31%) or pH 2.5 acid phosphatase (14%). These findings confirm that A. niger pH 2.5 acid phosphatase is irreversibly inactivated at temperatures above 80°C and that the capacity of A. fumigatus phytase to refold properly after heat denaturation may favorably affect its pelleting stability.

scholarly journals PURIFICATION OF GLUTARALDEHYDE ITS SIGNIFICANCE FOR PRESERVATION OF ACID PHOSPHATASE ACTIVITY

1968 ◽  
Vol 16 (3) ◽  
pp. 199-204 ◽  
Author(s):  
H. DARIUSH FAHIMI ◽  
PIERRE DROCHMANS ◽  
A. POPOWSKI
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Enzymatic Activity ◽  
Phosphatase Activity ◽  
Rat Liver ◽  
Acid Phosphatase Activity ◽  
High Concentration ◽  
Liver Homogenates ◽  
Inorganic Phosphates

The inhibition of acid phosphatase activity in rat liver homogenates after fixation in different lots of commercial glutaraldehyde is determined and compared with the inhibition following fixation with a distilled product. It is shown that commercial glutaraldehydes inhibit more of the enzyme activity than the distilled product. The acidic products of oxidation of glutaraldehyde do not increase the inhibition of the enzymatic activity. The presence of high concentration of inorganic phosphates in different lots of commercial glutaraldehyde, as presented here, suggests that probably such impurities may be responsible for increased inhibition of phosphatase activity noted after fixation in commercial glutaraldehydes.

Nuclear reverse T3 binding sites: an artefact of isolation?

1985 ◽  
Vol 108 (4) ◽  
pp. 525-531 ◽  
Author(s):  
R. Hartong ◽  
W. M. Wiersinga
Keyword(s):  
Rat Liver ◽  
Binding Sites ◽  
Reverse T3 ◽  
Nuclear Extracts ◽  
Ping Pong ◽  
Ionic Detergent ◽  
Enzymatic Nature ◽  
Triton X ◽  
Sulfhydryl Compounds

Abstract. Binding of [125I]rT3 to rat liver nuclear extracts prepared in 0.25 m sucrose could be abolished by a prior wash of the nuclei with 2.4 m sucrose. Analysis of mixtures containing [125I]rT3 and nuclear extracts (0.25 m sucrose) showed that after incubation for 2 h at 22°C, degradation of rT3 into 3,3'-T2 and I- had taken place. It appears that the presence of 125I- in these mixtures can account for the previously observed 'binding' of [125I]rT3 to these nuclear extracts. Further characterization of the deiodination process in nuclear extracts showed: 1) inactivation by heating, 2) production of equimolar amounts of I- and 3,3'-T2, 3) stimulation by sulfhydryl compounds and inhibition by propylthiouracil in a fashion similar to the microsomal iodothyronine 5'-deiodinase (ping-pong mechanism). We conclude that the observed deiodination of rT3 in hepatic nuclear extracts is of enzymatic nature, due to contamination of the nuclear preparation by microsomal iodothyronine 5'-deiodinase. However, since the nuclei are prepared in the presence of the non-ionic detergent Triton X-100, a nucleus associated deiodinase activity cannot be totally excluded.

Gas-Liquid Chromatography of Some Fatty Acid Esters and Alcohols in Lipsticks

1966 ◽  
Vol 49 (6) ◽  
pp. 1196-1200
Author(s):  
Frederick C Gross
Keyword(s):  
Liquid Chromatography ◽  
Oleyl Alcohol ◽  
Internal Standard ◽  
Standard Technique ◽  
Fatty Acid Esters ◽  
Isopropyl Myristate ◽  
Gas Liquid Chromatography ◽  
Triton X ◽  
Acid Esters

Abstract Gas-liquid chromatography (GLC) is used to separate and determine the lipstick ingredients: butyl stearate, oleyl alcohol, cetyl alcohol, isopropyl myristate, and isopropyl palmitate. The interfering hydrocarbons normally found in lipsticks are removed by column chromatography prior to the GLC analysis. Two columns, Triton X-405 on Fluoroport T and Carbowax 20M on Fluoroport T, are used in the procedure. Those ingredients which are not well separated on one of these columns will separate on the other. An internal standard technique is used for quantitative determination of the ingredients. Recoveries of 93–107% were obtained when known amounts of these compounds were carried through the procedure. Recoveries in the same range were obtained when the compounds were added to commercial lipsticks. The method should be applicable to the determination of these compounds in other types of cosmetics. It is recommended that study be continued.

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