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The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships: Structure/function relationships
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| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , , , , , , , , , |
| In: | European Journal of Biochemistry, 268, 2001, 14, S. 4104-4111 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Tamburrini, Maurizio Verde, Cinzia Olianas, Alessandra Giardina, Bruno Corda, Marcella Sanna, Maria T. Fais, Antonella Deiana, Anna M. di Prisco, Guido Pellegrini, Mariagiuseppina Tamburrini, Maurizio Verde, Cinzia Olianas, Alessandra Giardina, Bruno Corda, Marcella Sanna, Maria T. Fais, Antonella Deiana, Anna M. di Prisco, Guido Pellegrini, Mariagiuseppina |
|---|---|
| author |
Tamburrini, Maurizio Verde, Cinzia Olianas, Alessandra Giardina, Bruno Corda, Marcella Sanna, Maria T. Fais, Antonella Deiana, Anna M. di Prisco, Guido Pellegrini, Mariagiuseppina |
| spellingShingle |
Tamburrini, Maurizio Verde, Cinzia Olianas, Alessandra Giardina, Bruno Corda, Marcella Sanna, Maria T. Fais, Antonella Deiana, Anna M. di Prisco, Guido Pellegrini, Mariagiuseppina European Journal of Biochemistry The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships Biochemistry |
| author_sort |
tamburrini, maurizio |
| spelling |
Tamburrini, Maurizio Verde, Cinzia Olianas, Alessandra Giardina, Bruno Corda, Marcella Sanna, Maria T. Fais, Antonella Deiana, Anna M. di Prisco, Guido Pellegrini, Mariagiuseppina 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1046/j.1432-1327.2001.02333.x <jats:p>The <jats:italic>Gymnothorax unicolor</jats:italic> hemoglobin system is characterized by two components, called cathodic and anodic on the basis of their isoelectric point, which were separated by ion‐exchange chromatography. The oxygen‐binding properties of the purified components were studied in the absence and presence of chloride and/or GTP or ATP in the pH range 6.5–8.0. Stripped cathodic hemoglobin showed a small reverse Bohr effect, high oxygen affinity, and low co‐operativity; the addition of chloride only caused a small decrease in oxygen affinity. In the presence of GTP or ATP, the oxygen affinity was dramatically reduced, the co‐operativity increased, and the reverse Bohr effect abolished. Stripped anodic hemoglobin is characterized by both low oxygen affinity and co‐operativity, and displayed a normal Bohr effect; the addition of chloride increased co‐operativity, whereas ATP and GTP significantly modulated oxygen affinity at acidic pH values, enhancing the Bohr effect and giving rise to the Root effect. The complete amino‐acid sequences of the α and β chains of both hemoglobins were established; the molecular basis of the functional properties of the hemoglobins is discussed in the light of the primary structure and compared with those of other fish hemoglobins.</jats:p> Structure/function relationships The hemoglobin system of the brown moray <i>Gymnothorax unicolor</i> : Structure/function relationships European Journal of Biochemistry |
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2001 |
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European Journal of Biochemistry |
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49 |
| title_sub |
Structure/function relationships |
| title |
The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_unstemmed |
The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_full |
The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_fullStr |
The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_full_unstemmed |
The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_short |
The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_sort |
the hemoglobin system of the brown moray <i>gymnothorax unicolor</i> : structure/function relationships |
| topic |
Biochemistry |
| url |
http://dx.doi.org/10.1046/j.1432-1327.2001.02333.x |
| publishDate |
2001 |
| physical |
4104-4111 |
| description |
<jats:p>The <jats:italic>Gymnothorax unicolor</jats:italic> hemoglobin system is characterized by two components, called cathodic and anodic on the basis of their isoelectric point, which were separated by ion‐exchange chromatography. The oxygen‐binding properties of the purified components were studied in the absence and presence of chloride and/or GTP or ATP in the pH range 6.5–8.0. Stripped cathodic hemoglobin showed a small reverse Bohr effect, high oxygen affinity, and low co‐operativity; the addition of chloride only caused a small decrease in oxygen affinity. In the presence of GTP or ATP, the oxygen affinity was dramatically reduced, the co‐operativity increased, and the reverse Bohr effect abolished. Stripped anodic hemoglobin is characterized by both low oxygen affinity and co‐operativity, and displayed a normal Bohr effect; the addition of chloride increased co‐operativity, whereas ATP and GTP significantly modulated oxygen affinity at acidic pH values, enhancing the Bohr effect and giving rise to the Root effect. The complete amino‐acid sequences of the α and β chains of both hemoglobins were established; the molecular basis of the functional properties of the hemoglobins is discussed in the light of the primary structure and compared with those of other fish hemoglobins.</jats:p> |
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| author | Tamburrini, Maurizio, Verde, Cinzia, Olianas, Alessandra, Giardina, Bruno, Corda, Marcella, Sanna, Maria T., Fais, Antonella, Deiana, Anna M., di Prisco, Guido, Pellegrini, Mariagiuseppina |
| author_facet | Tamburrini, Maurizio, Verde, Cinzia, Olianas, Alessandra, Giardina, Bruno, Corda, Marcella, Sanna, Maria T., Fais, Antonella, Deiana, Anna M., di Prisco, Guido, Pellegrini, Mariagiuseppina, Tamburrini, Maurizio, Verde, Cinzia, Olianas, Alessandra, Giardina, Bruno, Corda, Marcella, Sanna, Maria T., Fais, Antonella, Deiana, Anna M., di Prisco, Guido, Pellegrini, Mariagiuseppina |
| author_sort | tamburrini, maurizio |
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| description | <jats:p>The <jats:italic>Gymnothorax unicolor</jats:italic> hemoglobin system is characterized by two components, called cathodic and anodic on the basis of their isoelectric point, which were separated by ion‐exchange chromatography. The oxygen‐binding properties of the purified components were studied in the absence and presence of chloride and/or GTP or ATP in the pH range 6.5–8.0. Stripped cathodic hemoglobin showed a small reverse Bohr effect, high oxygen affinity, and low co‐operativity; the addition of chloride only caused a small decrease in oxygen affinity. In the presence of GTP or ATP, the oxygen affinity was dramatically reduced, the co‐operativity increased, and the reverse Bohr effect abolished. Stripped anodic hemoglobin is characterized by both low oxygen affinity and co‐operativity, and displayed a normal Bohr effect; the addition of chloride increased co‐operativity, whereas ATP and GTP significantly modulated oxygen affinity at acidic pH values, enhancing the Bohr effect and giving rise to the Root effect. The complete amino‐acid sequences of the α and β chains of both hemoglobins were established; the molecular basis of the functional properties of the hemoglobins is discussed in the light of the primary structure and compared with those of other fish hemoglobins.</jats:p> |
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| imprint | Wiley, 2001 |
| imprint_str_mv | Wiley, 2001 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| physical | 4104-4111 |
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| series | European Journal of Biochemistry |
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| spelling | Tamburrini, Maurizio Verde, Cinzia Olianas, Alessandra Giardina, Bruno Corda, Marcella Sanna, Maria T. Fais, Antonella Deiana, Anna M. di Prisco, Guido Pellegrini, Mariagiuseppina 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1046/j.1432-1327.2001.02333.x <jats:p>The <jats:italic>Gymnothorax unicolor</jats:italic> hemoglobin system is characterized by two components, called cathodic and anodic on the basis of their isoelectric point, which were separated by ion‐exchange chromatography. The oxygen‐binding properties of the purified components were studied in the absence and presence of chloride and/or GTP or ATP in the pH range 6.5–8.0. Stripped cathodic hemoglobin showed a small reverse Bohr effect, high oxygen affinity, and low co‐operativity; the addition of chloride only caused a small decrease in oxygen affinity. In the presence of GTP or ATP, the oxygen affinity was dramatically reduced, the co‐operativity increased, and the reverse Bohr effect abolished. Stripped anodic hemoglobin is characterized by both low oxygen affinity and co‐operativity, and displayed a normal Bohr effect; the addition of chloride increased co‐operativity, whereas ATP and GTP significantly modulated oxygen affinity at acidic pH values, enhancing the Bohr effect and giving rise to the Root effect. The complete amino‐acid sequences of the α and β chains of both hemoglobins were established; the molecular basis of the functional properties of the hemoglobins is discussed in the light of the primary structure and compared with those of other fish hemoglobins.</jats:p> Structure/function relationships The hemoglobin system of the brown moray <i>Gymnothorax unicolor</i> : Structure/function relationships European Journal of Biochemistry |
| spellingShingle | Tamburrini, Maurizio, Verde, Cinzia, Olianas, Alessandra, Giardina, Bruno, Corda, Marcella, Sanna, Maria T., Fais, Antonella, Deiana, Anna M., di Prisco, Guido, Pellegrini, Mariagiuseppina, European Journal of Biochemistry, The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships, Biochemistry |
| title | The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_full | The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_fullStr | The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_full_unstemmed | The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_short | The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| title_sort | the hemoglobin system of the brown moray <i>gymnothorax unicolor</i> : structure/function relationships |
| title_sub | Structure/function relationships |
| title_unstemmed | The hemoglobin system of the brown moray Gymnothorax unicolor : Structure/function relationships |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1046/j.1432-1327.2001.02333.x |