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Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification
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| Zeitschriftentitel: | Bioscience Reports |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Bioscience Reports, 4, 1984, 7, S. 573-579 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
|
| Schlagwörter: |
| author_facet |
Tashian, Richard E. Johansen, Jack T. Christiansen, Erik Chegwidden, W. Richard Tashian, Richard E. Johansen, Jack T. Christiansen, Erik Chegwidden, W. Richard |
|---|---|
| author |
Tashian, Richard E. Johansen, Jack T. Christiansen, Erik Chegwidden, W. Richard |
| spellingShingle |
Tashian, Richard E. Johansen, Jack T. Christiansen, Erik Chegwidden, W. Richard Bioscience Reports Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification Cell Biology Molecular Biology Biochemistry Biophysics |
| author_sort |
tashian, richard e. |
| spelling |
Tashian, Richard E. Johansen, Jack T. Christiansen, Erik Chegwidden, W. Richard 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1007/bf01121914 <jats:p>Purified carbonic anhydrase isozymes I, II, and III (CA I, CA II, CA III) from various sources were treated with 2,3-butanedione and their bicarbonate dehydration reactions followed. The specific activities of human and bovine CA I and CA II and chicken CA III were not affected by the butanedione treatment, whereas the activities of human, gorilla, and bovine CA III were rapidly activated. These findings suggest that one, or both, of the two arginyl residues which appear to be unique to the active sites of the mammalian CA III isozymes are modified by butanedione.</jats:p> Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification Bioscience Reports |
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Portland Press Ltd., 1984 |
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Portland Press Ltd., 1984 |
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1984 |
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Portland Press Ltd. |
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Bioscience Reports |
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49 |
| title |
Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_unstemmed |
Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_full |
Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_fullStr |
Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_full_unstemmed |
Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_short |
Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_sort |
activation of mammalian skeletal-muscle carbonic anhydrase iii by arginine modification |
| topic |
Cell Biology Molecular Biology Biochemistry Biophysics |
| url |
http://dx.doi.org/10.1007/bf01121914 |
| publishDate |
1984 |
| physical |
573-579 |
| description |
<jats:p>Purified carbonic anhydrase isozymes I, II, and III (CA I, CA II, CA III) from various sources were treated with 2,3-butanedione and their bicarbonate dehydration reactions followed. The specific activities of human and bovine CA I and CA II and chicken CA III were not affected by the butanedione treatment, whereas the activities of human, gorilla, and bovine CA III were rapidly activated. These findings suggest that one, or both, of the two arginyl residues which appear to be unique to the active sites of the mammalian CA III isozymes are modified by butanedione.</jats:p> |
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| author | Tashian, Richard E., Johansen, Jack T., Christiansen, Erik, Chegwidden, W. Richard |
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| description | <jats:p>Purified carbonic anhydrase isozymes I, II, and III (CA I, CA II, CA III) from various sources were treated with 2,3-butanedione and their bicarbonate dehydration reactions followed. The specific activities of human and bovine CA I and CA II and chicken CA III were not affected by the butanedione treatment, whereas the activities of human, gorilla, and bovine CA III were rapidly activated. These findings suggest that one, or both, of the two arginyl residues which appear to be unique to the active sites of the mammalian CA III isozymes are modified by butanedione.</jats:p> |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAwNy9iZjAxMTIxOTE0 |
| imprint | Portland Press Ltd., 1984 |
| imprint_str_mv | Portland Press Ltd., 1984 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229 |
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| language | English |
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| mega_collection | Portland Press Ltd. (CrossRef) |
| physical | 573-579 |
| publishDate | 1984 |
| publishDateSort | 1984 |
| publisher | Portland Press Ltd. |
| record_format | ai |
| recordtype | ai |
| series | Bioscience Reports |
| source_id | 49 |
| spelling | Tashian, Richard E. Johansen, Jack T. Christiansen, Erik Chegwidden, W. Richard 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1007/bf01121914 <jats:p>Purified carbonic anhydrase isozymes I, II, and III (CA I, CA II, CA III) from various sources were treated with 2,3-butanedione and their bicarbonate dehydration reactions followed. The specific activities of human and bovine CA I and CA II and chicken CA III were not affected by the butanedione treatment, whereas the activities of human, gorilla, and bovine CA III were rapidly activated. These findings suggest that one, or both, of the two arginyl residues which appear to be unique to the active sites of the mammalian CA III isozymes are modified by butanedione.</jats:p> Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification Bioscience Reports |
| spellingShingle | Tashian, Richard E., Johansen, Jack T., Christiansen, Erik, Chegwidden, W. Richard, Bioscience Reports, Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification, Cell Biology, Molecular Biology, Biochemistry, Biophysics |
| title | Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_full | Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_fullStr | Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_full_unstemmed | Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_short | Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| title_sort | activation of mammalian skeletal-muscle carbonic anhydrase iii by arginine modification |
| title_unstemmed | Activation of mammalian skeletal-muscle carbonic anhydrase III by arginine modification |
| topic | Cell Biology, Molecular Biology, Biochemistry, Biophysics |
| url | http://dx.doi.org/10.1007/bf01121914 |