Haemoglobin Tak: a β‐Chain Elongation
In Haemoglobin Tak two normal α‐chains are combined with two β‐chains elongated by 11 residues beyond the C‐terminus. Unlike in the α‐chain abnormal Hb Constant Spring, the elongation cannot result from a point mutation of a stop codon. It is probably due to an unequal crossing‐over near the 3′ end...
Saved in:
Main Authors: | , , , , , , , |
---|---|
Other Authors: | |
Format: | Article |
Published: |
2018
|
Subjects: | |
Online Access: | https://repository.li.mahidol.ac.th/handle/123456789/10823 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Mahidol University |
id |
th-mahidol.10823 |
---|---|
record_format |
dspace |
spelling |
th-mahidol.108232018-04-19T21:09:30Z Haemoglobin Tak: a β‐Chain Elongation H. Lehmann R. Casey A. Lang R. Stathopoulou K. Imai S. Tuchinda P. Vinai G. Flatz University of Cambridge Mahidol University Medizinische Hochschule Hannover (MHH) Medicine In Haemoglobin Tak two normal α‐chains are combined with two β‐chains elongated by 11 residues beyond the C‐terminus. Unlike in the α‐chain abnormal Hb Constant Spring, the elongation cannot result from a point mutation of a stop codon. It is probably due to an unequal crossing‐over near the 3′ end of the β‐chain structural gene. This could cause either a deletion of the normal stop codon or a shift in the reading frame. Oxygen dissociation of purified Hb Tak shows no cooperativity but in Hb A + Tak haemolysates there is no interaction between the two above 40% O 2 saturation. Heterozygotes for Hbs A and Tak show an imbalance of globin chain synthesis (α/non α= 1.5), the synthesis of β Tak resembles that of the β‐chain in β + thalassaemia. Copyright © 1975, Wiley Blackwell. All rights reserved 2018-04-19T14:09:30Z 2018-04-19T14:09:30Z 1975-01-01 Article British Journal of Haematology. Vol.31, (1975), 119-131 10.1111/j.1365-2141.1975.tb00905.x 13652141 00071048 2-s2.0-84990439389 https://repository.li.mahidol.ac.th/handle/123456789/10823 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84990439389&origin=inward |
institution |
Mahidol University |
building |
Mahidol University Library |
continent |
Asia |
country |
Thailand Thailand |
content_provider |
Mahidol University Library |
collection |
Mahidol University Institutional Repository |
topic |
Medicine |
spellingShingle |
Medicine H. Lehmann R. Casey A. Lang R. Stathopoulou K. Imai S. Tuchinda P. Vinai G. Flatz Haemoglobin Tak: a β‐Chain Elongation |
description |
In Haemoglobin Tak two normal α‐chains are combined with two β‐chains elongated by 11 residues beyond the C‐terminus. Unlike in the α‐chain abnormal Hb Constant Spring, the elongation cannot result from a point mutation of a stop codon. It is probably due to an unequal crossing‐over near the 3′ end of the β‐chain structural gene. This could cause either a deletion of the normal stop codon or a shift in the reading frame. Oxygen dissociation of purified Hb Tak shows no cooperativity but in Hb A + Tak haemolysates there is no interaction between the two above 40% O 2 saturation. Heterozygotes for Hbs A and Tak show an imbalance of globin chain synthesis (α/non α= 1.5), the synthesis of β Tak resembles that of the β‐chain in β + thalassaemia. Copyright © 1975, Wiley Blackwell. All rights reserved |
author2 |
University of Cambridge |
author_facet |
University of Cambridge H. Lehmann R. Casey A. Lang R. Stathopoulou K. Imai S. Tuchinda P. Vinai G. Flatz |
format |
Article |
author |
H. Lehmann R. Casey A. Lang R. Stathopoulou K. Imai S. Tuchinda P. Vinai G. Flatz |
author_sort |
H. Lehmann |
title |
Haemoglobin Tak: a β‐Chain Elongation |
title_short |
Haemoglobin Tak: a β‐Chain Elongation |
title_full |
Haemoglobin Tak: a β‐Chain Elongation |
title_fullStr |
Haemoglobin Tak: a β‐Chain Elongation |
title_full_unstemmed |
Haemoglobin Tak: a β‐Chain Elongation |
title_sort |
haemoglobin tak: a β‐chain elongation |
publishDate |
2018 |
url |
https://repository.li.mahidol.ac.th/handle/123456789/10823 |
_version_ |
1763494668094406656 |