Novel haemoglobin mutation (α127Lys→Glu) increases oxygen affinity and has a minor effect on haptoglobin binding-Reference-Cited by-同舟云学术

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Novel haemoglobin mutation (α127Lys→Glu) increases oxygen affinity and has a minor effect on haptoglobin binding

Published:2012-12 Issue:18 Volume:45 Page:1587-1590
ISSN:0009-9120
Container-title:Clinical Biochemistry
language:en
Short-container-title:Clinical Biochemistry

Author:

Brennan Stephen O.,Pullon Beverley,Owen Maurice C.,Brittain Thomas

Publisher

Elsevier BV

Subject

Clinical Biochemistry,General Medicine

Reference10 articles.

1. Fifty-eight years of hemoglobin analysis;Brennan;Clin Chem,2008

2. In ‘Human Hemoglobins’;Bunn,1997

3. Hemoglobin binding with haptoglobin: delineation of the haptoglobin binding site on the alpha-chain of human hemoglobin;McCormick;J Protein Chem,1990

4. β37Trp→Cys mutation leads to multiple new hemoglobin species in red cells;Brennan;Clin Biochem,2012

5. Hb Auckland (α87 His→Asn): a new mutation of the proximal histidine identified by electrospray mass spectrometry;Brennan;Hemoglobin,1997

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Erythrocytosis: genes and pathways involved in disease development;BLOOD TRANSFUS-ITALY;2021

2. Hb Waikato [α127(H10)Lys→Gln; HBA1: c.382A>C]: A Novel High Oxygen Affinity Variant;Hemoglobin;2021-01-02

3. Hb I-Toulouse in Association with Homozygosity for the α3.7 Deletion in a Pacific Island Woman;Thalassemia Reports;2016-11-30

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