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Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid
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| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , , |
| In: | European Journal of Biochemistry, 187, 1990, 3, S. 713-719 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
HITOMI, Masahiro ODANI, Shoji ONO, Teruo HITOMI, Masahiro ODANI, Shoji ONO, Teruo |
|---|---|
| author |
HITOMI, Masahiro ODANI, Shoji ONO, Teruo |
| spellingShingle |
HITOMI, Masahiro ODANI, Shoji ONO, Teruo European Journal of Biochemistry Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid Biochemistry |
| author_sort |
hitomi, masahiro |
| spelling |
HITOMI, Masahiro ODANI, Shoji ONO, Teruo 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1990.tb15358.x <jats:p>0.16 ± 0.062% of the fatty acid‐binding protein purified from 50 mM <jats:italic>N</jats:italic>‐ethylmaleimide‐treated rat liver (L‐FABP) was determined as a form <jats:italic>S</jats:italic>‐thiolated by glutathione (L‐FABP‐SSG). L‐FABP‐SSG, which was prepared <jats:italic>in vitro</jats:italic> through thiol – disulfide exchange reaction, showed more acidic pI (∼ 5.0) than the pI (∼ 7.0) of reduced L‐FABP. <jats:italic>S</jats:italic>‐thiolation of L‐FABP by glutathione decreased the affinity of the protein for unsaturated fatty acids without changing the equimolar maximum binding. The changes in <jats:italic>K</jats:italic><jats:sub>d</jats:sub> were from 0.63 ± 0.054 μM to 1.03 ± 0.14 μM for oleic acid, from 0.63 ± 0.028 μM to 0.97 ± 0.12 μM for linoleic acid and from 0.85 ± 0.050 μM to 1.45 ± 0.024 μM for arachidonic acid. This modification did not alter the affinity nor the maximum binding for saturated fatty acids, which were determined to be <jats:italic>K</jats:italic><jats:sub>d</jats:sub> of ∼ 1.0 μM for palmitic acid and ∼ 0.9 μM for stearic acids, and equimolar maximum binding for both fatty acids. The binding affinity of L‐FABP for unsaturated fatty acid may be regulated by redox state of the liver.</jats:p> Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid European Journal of Biochemistry |
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10.1111/j.1432-1033.1990.tb15358.x |
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Online Free |
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Chemie und Pharmazie |
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Wiley, 1990 |
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Wiley, 1990 |
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0014-2956 1432-1033 |
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0014-2956 1432-1033 |
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1990 |
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Wiley |
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European Journal of Biochemistry |
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49 |
| title |
Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_unstemmed |
Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_full |
Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_fullStr |
Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_full_unstemmed |
Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_short |
Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_sort |
glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| topic |
Biochemistry |
| url |
http://dx.doi.org/10.1111/j.1432-1033.1990.tb15358.x |
| publishDate |
1990 |
| physical |
713-719 |
| description |
<jats:p>0.16 ± 0.062% of the fatty acid‐binding protein purified from 50 mM <jats:italic>N</jats:italic>‐ethylmaleimide‐treated rat liver (L‐FABP) was determined as a form <jats:italic>S</jats:italic>‐thiolated by glutathione (L‐FABP‐SSG). L‐FABP‐SSG, which was prepared <jats:italic>in vitro</jats:italic> through thiol – disulfide exchange reaction, showed more acidic pI (∼ 5.0) than the pI (∼ 7.0) of reduced L‐FABP. <jats:italic>S</jats:italic>‐thiolation of L‐FABP by glutathione decreased the affinity of the protein for unsaturated fatty acids without changing the equimolar maximum binding. The changes in <jats:italic>K</jats:italic><jats:sub>d</jats:sub> were from 0.63 ± 0.054 μM to 1.03 ± 0.14 μM for oleic acid, from 0.63 ± 0.028 μM to 0.97 ± 0.12 μM for linoleic acid and from 0.85 ± 0.050 μM to 1.45 ± 0.024 μM for arachidonic acid. This modification did not alter the affinity nor the maximum binding for saturated fatty acids, which were determined to be <jats:italic>K</jats:italic><jats:sub>d</jats:sub> of ∼ 1.0 μM for palmitic acid and ∼ 0.9 μM for stearic acids, and equimolar maximum binding for both fatty acids. The binding affinity of L‐FABP for unsaturated fatty acid may be regulated by redox state of the liver.</jats:p> |
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| author | HITOMI, Masahiro, ODANI, Shoji, ONO, Teruo |
| author_facet | HITOMI, Masahiro, ODANI, Shoji, ONO, Teruo, HITOMI, Masahiro, ODANI, Shoji, ONO, Teruo |
| author_sort | hitomi, masahiro |
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| container_title | European Journal of Biochemistry |
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| description | <jats:p>0.16 ± 0.062% of the fatty acid‐binding protein purified from 50 mM <jats:italic>N</jats:italic>‐ethylmaleimide‐treated rat liver (L‐FABP) was determined as a form <jats:italic>S</jats:italic>‐thiolated by glutathione (L‐FABP‐SSG). L‐FABP‐SSG, which was prepared <jats:italic>in vitro</jats:italic> through thiol – disulfide exchange reaction, showed more acidic pI (∼ 5.0) than the pI (∼ 7.0) of reduced L‐FABP. <jats:italic>S</jats:italic>‐thiolation of L‐FABP by glutathione decreased the affinity of the protein for unsaturated fatty acids without changing the equimolar maximum binding. The changes in <jats:italic>K</jats:italic><jats:sub>d</jats:sub> were from 0.63 ± 0.054 μM to 1.03 ± 0.14 μM for oleic acid, from 0.63 ± 0.028 μM to 0.97 ± 0.12 μM for linoleic acid and from 0.85 ± 0.050 μM to 1.45 ± 0.024 μM for arachidonic acid. This modification did not alter the affinity nor the maximum binding for saturated fatty acids, which were determined to be <jats:italic>K</jats:italic><jats:sub>d</jats:sub> of ∼ 1.0 μM for palmitic acid and ∼ 0.9 μM for stearic acids, and equimolar maximum binding for both fatty acids. The binding affinity of L‐FABP for unsaturated fatty acid may be regulated by redox state of the liver.</jats:p> |
| doi_str_mv | 10.1111/j.1432-1033.1990.tb15358.x |
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| format_dezwi2 | Article, E-Article |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4xOTkwLnRiMTUzNTgueA |
| imprint | Wiley, 1990 |
| imprint_str_mv | Wiley, 1990 |
| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
| issn | 0014-2956, 1432-1033 |
| issn_str_mv | 0014-2956, 1432-1033 |
| language | English |
| last_indexed | 2024-03-01T15:18:51.849Z |
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| mega_collection | Wiley (CrossRef) |
| physical | 713-719 |
| publishDate | 1990 |
| publishDateSort | 1990 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | European Journal of Biochemistry |
| source_id | 49 |
| spelling | HITOMI, Masahiro ODANI, Shoji ONO, Teruo 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1990.tb15358.x <jats:p>0.16 ± 0.062% of the fatty acid‐binding protein purified from 50 mM <jats:italic>N</jats:italic>‐ethylmaleimide‐treated rat liver (L‐FABP) was determined as a form <jats:italic>S</jats:italic>‐thiolated by glutathione (L‐FABP‐SSG). L‐FABP‐SSG, which was prepared <jats:italic>in vitro</jats:italic> through thiol – disulfide exchange reaction, showed more acidic pI (∼ 5.0) than the pI (∼ 7.0) of reduced L‐FABP. <jats:italic>S</jats:italic>‐thiolation of L‐FABP by glutathione decreased the affinity of the protein for unsaturated fatty acids without changing the equimolar maximum binding. The changes in <jats:italic>K</jats:italic><jats:sub>d</jats:sub> were from 0.63 ± 0.054 μM to 1.03 ± 0.14 μM for oleic acid, from 0.63 ± 0.028 μM to 0.97 ± 0.12 μM for linoleic acid and from 0.85 ± 0.050 μM to 1.45 ± 0.024 μM for arachidonic acid. This modification did not alter the affinity nor the maximum binding for saturated fatty acids, which were determined to be <jats:italic>K</jats:italic><jats:sub>d</jats:sub> of ∼ 1.0 μM for palmitic acid and ∼ 0.9 μM for stearic acids, and equimolar maximum binding for both fatty acids. The binding affinity of L‐FABP for unsaturated fatty acid may be regulated by redox state of the liver.</jats:p> Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid European Journal of Biochemistry |
| spellingShingle | HITOMI, Masahiro, ODANI, Shoji, ONO, Teruo, European Journal of Biochemistry, Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid, Biochemistry |
| title | Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_full | Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_fullStr | Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_full_unstemmed | Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_short | Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_sort | glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| title_unstemmed | Glutathione‐protein mixed disulfide decreases the affinity of rat liver fatty acid‐binding protein for unsaturated fatty acid |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1111/j.1432-1033.1990.tb15358.x |