Chemical characterization of haemoglobin G-St-I
In: Nature, Jg. 211 (1966-09-17), Heft 5055
Online
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Zugriff:
AMONG the genetic variants of adult human haemoglobin, some thirteen amino-acid substitutions have been described which occur along the primary sequence of the α-polypeptide chain. The most widespread and frequently encountered α-chain variant is the substitution of lysine for asparagine in the 68th residue of haemoglobin A (ref. 1). A structural mutation leading to the substitution of asparagine by lysine in a protein can be the direct result of a single nucleotide base alteration within the triplet code. Here an alteration in triplet AAU or AAC specifying asparagine could result in AAA or AAG which code for lysine2. Haemoglobin variants carrying a substitution of lysine for asparagine in the 68th residue of the polypeptide chain have been described in Negro families living in Philadelphia1, Bristol3, Azuokoli, St. Louis, Washington and Baltimore4, and Knoxville6.
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Chemical characterization of haemoglobin G-St-I
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Autor/in / Beteiligte Person: | Hodgkinson, Katherine T. ; Bowman, Barbara H. ; Barnett, D.R. ; Schneider, Rose G. |
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Zeitschrift: | Nature, Jg. 211 (1966-09-17), Heft 5055 |
Veröffentlichung: | 1966 |
Medientyp: | unknown |
ISSN: | 0028-0836 (print) |
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