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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/10823
Title: Haemoglobin Tak: a β‐Chain Elongation
Authors: 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)
Keywords: Medicine
Issue Date: 1-Jan-1975
Citation: British Journal of Haematology. Vol.31, (1975), 119-131
Abstract: 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
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84990439389&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/10823
ISSN: 13652141
00071048
Appears in Collections:Scopus 1969-1990

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