Latency of epoxide hydratase and its relationship to that of udpglucuronyltransferase
Epoxide hydratase activity in liver microsomal preparations from adult male rats is latent to a slight extent. Maximal activations with neutral or anionic detergents were 30–60% whilst UDPglucuronyltransferase was maximally activated by 160–830% by the same detergents. Activation of microsomal epoxi...
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| Published in | Biochimica et biophysica acta Vol. 444; no. 2; pp. 531 - 538 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
24.09.1976
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| Subjects | |
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| Abstract | Epoxide hydratase activity in liver microsomal preparations from adult male rats is latent to a slight extent. Maximal activations with neutral or anionic detergents were 30–60% whilst UDPglucuronyltransferase was maximally activated by 160–830% by the same detergents. Activation of microsomal epoxide hydratase requires much higher amounts of neutral or anionic detergents than activation of microsomal UDPglucuronyltransferase. High concentrations of inorganic salt, sonication or freeze-thawing which activate microsomal UDPglucuronyltransferase have no influence on microsomal epoxide hydratase activity. From this it appears that the activation which may involve either removal of a permeability barrier or release from conformational restraint occurs more easily for UDPglucuronyltransferase than for epoxide hydratase and that the activation of microsomal epoxide hydratase requires breakage of some hydrophobic bonds between the enzyme and membrane components(s). |
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| AbstractList | Epoxide hydratase activity in liver microsomal preparations from adult made rats is latent to a slight extent. Maximal activations with neutral or anionic detergents were 30-60% whilst UDPglucuronyltransferase was maximally activated by 160-830% by the same detergents. Activation of microsomal epoxide hydratase requires much higher amounts of neutral or anionic detergents than activation of microsomal UDPglucuronyltransferase. High concentrations of inorganic salt, sonication or freeze-thawing which activate microsomal UDPglucuronyltransferase have no influence on microsomal epoxide hydratase activity. From this it appears that the activation which may involve either removal of a permeability barrier or release from conformational restraint occurs more easily for UDPglucuronyltransferase than for epoxide hydratase and that the activation of microsomal epoxide hydratase requires breakage of some hydrophobic bonds between the enzyme and membrrane component(s). Epoxide hydratase activity in liver microsomal preparations from adult made rats is latent to a slight extent. Maximal activations with neutral or anionic detergents were 30-60% whilst UDPglucuronyltransferase was maximally activated by 160-830% by the same detergents. Activation of microsomal epoxide hydratase requires much higher amounts of neutral or anionic detergents than activation of microsomal UDPglucuronyltransferase. High concentrations of inorganic salt, sonication or freeze-thawing which activate microsomal UDPglucuronyltransferase have no influence on microsomal epoxide hydratase activity. From this it appears that the activation which may involve either removal of a permeability barrier or release from conformational restraint occurs more easily for UDPglucuronyltransferase than for epoxide hydratase and that the activation of microsomal epoxide hydratase requires breakage of some hydrophobic bonds between the enzyme and membrrane component(s).Epoxide hydratase activity in liver microsomal preparations from adult made rats is latent to a slight extent. Maximal activations with neutral or anionic detergents were 30-60% whilst UDPglucuronyltransferase was maximally activated by 160-830% by the same detergents. Activation of microsomal epoxide hydratase requires much higher amounts of neutral or anionic detergents than activation of microsomal UDPglucuronyltransferase. High concentrations of inorganic salt, sonication or freeze-thawing which activate microsomal UDPglucuronyltransferase have no influence on microsomal epoxide hydratase activity. From this it appears that the activation which may involve either removal of a permeability barrier or release from conformational restraint occurs more easily for UDPglucuronyltransferase than for epoxide hydratase and that the activation of microsomal epoxide hydratase requires breakage of some hydrophobic bonds between the enzyme and membrrane component(s). Epoxide hydratase activity in liver microsomal preparations from adult male rats is latent to a slight extent. Maximal activations with neutral or anionic detergents were 30–60% whilst UDPglucuronyltransferase was maximally activated by 160–830% by the same detergents. Activation of microsomal epoxide hydratase requires much higher amounts of neutral or anionic detergents than activation of microsomal UDPglucuronyltransferase. High concentrations of inorganic salt, sonication or freeze-thawing which activate microsomal UDPglucuronyltransferase have no influence on microsomal epoxide hydratase activity. From this it appears that the activation which may involve either removal of a permeability barrier or release from conformational restraint occurs more easily for UDPglucuronyltransferase than for epoxide hydratase and that the activation of microsomal epoxide hydratase requires breakage of some hydrophobic bonds between the enzyme and membrane components(s). |
| Author | Oesch, F. Burchell, B. Bentley, P. |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/822881$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1111_j_1600_0773_1980_tb02416_x crossref_primary_10_1111_j_1432_1033_1981_tb05335_x crossref_primary_10_1016_S0021_9258_18_50338_0 crossref_primary_10_1016_0006_2952_79_90082_0 crossref_primary_10_1016_0005_2760_90_90091_B crossref_primary_10_1016_0006_2952_84_90412_X crossref_primary_10_1111_j_1432_1033_1982_tb06797_x crossref_primary_10_1016_0003_2697_87_90227_2 crossref_primary_10_1016_0020_711X_79_90020_X crossref_primary_10_1016_0006_291X_86_90778_3 crossref_primary_10_1080_01635587909513603 crossref_primary_10_1007_BF00766870 crossref_primary_10_1007_s00204_013_1090_9 crossref_primary_10_1016_0005_2744_79_90313_9 crossref_primary_10_1111_j_1432_1033_1979_tb13112_x crossref_primary_10_1016_0020_1790_80_90058_X crossref_primary_10_1016_0304_419X_83_90014_8 crossref_primary_10_1016_S0021_9258_17_42429_X crossref_primary_10_1016_0006_2952_79_90200_4 crossref_primary_10_1016_0003_9861_80_90311_2 |
| Cites_doi | 10.1016/S0076-6879(62)05199-X 10.1016/0005-2744(71)90017-9 10.1016/0005-2744(72)90135-0 10.1016/0006-2952(73)90390-0 10.1042/bj1290605 10.1016/0005-2744(69)90247-2 10.1016/0005-2736(73)90253-8 10.1007/BF01946135 10.1016/0005-2744(72)90197-0 10.1016/0005-2744(71)90018-0 10.3109/00498257309151525 10.1016/S0065-230X(08)60111-6 10.1007/BF00499191 10.1042/bj1250991 10.1042/bj1390077 10.1016/0024-3205(70)90351-6 10.1038/255512a0 10.1016/0005-2736(73)90033-3 10.1016/S0021-9258(19)52451-6 10.1042/bst0021167 10.1042/bj0770182 10.1021/bi00803a019 |
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| SubjectTerms | Animals Deoxycholic Acid - pharmacology Detergents - pharmacology Enzyme Activation Epoxide Hydrolases - metabolism Freezing Glucuronosyltransferase - metabolism Hexosyltransferases - metabolism Hydro-Lyases - metabolism Male Microsomes, Liver - enzymology Potassium Chloride - pharmacology Rats Sodium Dodecyl Sulfate - pharmacology Sonication |
| Title | Latency of epoxide hydratase and its relationship to that of udpglucuronyltransferase |
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