Abstract |
Hemoglobin Brisbane is a new hemoglobin variant which produces a mile erythrocytosis. It is not detectable by electrophoresis at pH 8.6 or by isoelectric focusing but it is mildly unstable and gives a positive result with standard stability tests. The new hemoglobin has increased oxygen affinity and reduced co-operativity with a normal Bohr effect and 2,3-DPG binding. Structural analysis shows that a histidine residue has replaced the leucine normally found at position beta 68 (E12).
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Authors | S O Brennan, R M Wells, H Smith, R W Carrell |
Journal | Hemoglobin
(Hemoglobin)
Vol. 5
Issue 4
Pg. 325-35
( 1981)
ISSN: 0363-0269 [Print] England |
PMID | 6166590
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Diphosphoglyceric Acids
- Hemoglobins, Abnormal
- Peptides
- hemoglobin Brisbane
- Hemoglobin A
- Fetal Hemoglobin
- Trypsin
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Topics |
- Adult
- Amino Acid Sequence
- Australia
- Diphosphoglyceric Acids
(blood)
- Female
- Fetal Hemoglobin
- Genetic Variation
- Hemoglobin A
- Hemoglobins, Abnormal
- Humans
- Male
- Middle Aged
- Oxygen Consumption
- Peptides
- Trypsin
(pharmacology)
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