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Characterization of the binding of the anti-sickling compound, BW12C, to haemoglobin.

Abstract:

The anti-sickling agent BW12C [Beddell, Goodford, Kneen, White, Wilkinson and Wootton (1984) Br. J. Pharmacol. 82, 397-407] was designed to left-shift the oxygen saturation curve of haemoglobin (HbA) by preferential binding to the oxy conformation at a single site between the terminal amino groups of the alpha-chains through Schiff's base formation, ionic and hydrophobic interactions. In the present work, Schiff's base linkages formed with [14C]BW12C were reduced with NaBH4 and the alpha- and...

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Publication status:
Published

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Authors


Merrett, M More by this author
Stammers, DK More by this author
Wootton, R More by this author
Journal:
The Biochemical journal
Volume:
239
Issue:
2
Pages:
387-392
Publication date:
1986-10-05
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:4add5ed7-c57d-472f-b25e-7c93d7dc4588
Source identifiers:
72664
Local pid:
pubs:72664

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