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An Unstable Haemoglobin with Reduced Oxygen Affinity: Haemoglobin Peterborough, (βiii (G13) Valine → Phenylalanine, its Interaction with Normal Haemoglobin and with Haemoglobin Lepore
Author(s) -
King Marguerite A. R.,
Wiltshire Barbara G.,
Lehmann H.,
Morimoto H.
Publication year - 1972
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1972.tb08794.x
Subject(s) - bohr effect , heterozygote advantage , phenylalanine , valine , identical twins , chemistry , genetics , hemoglobin , biochemistry , biology , amino acid , genotype , oxygen–haemoglobin dissociation curve , gene
Summary: A new unstable haemoglobin, Hb Peterborough, is described in father and son. In the former it was found with Hb A but in the latter with Hb Lepore, the mother being a heterozygote for Hb A and Hb Lepore Boston (or Washington). In this respect it differs from other unstable haemoglobins so far described which have been observed in heterozygotes together with normal adult haemoglobin. It was therefore possible to compare the clinical and biochemical interactions of Hbs A and Peterborough, A and Lepore, and Peterborough and Lepore. Hb Peterborough has been identified as βiii (G‐13) Val → Phe. It has a low oxygen affinity, but the Bohr effect and haem‐haem interaction appear to be normal.