Hemoglobin F-Cincinnati, α2Gγ2 41(C7) Phe → Ser in a newborn with cyanosis

Ser at residue 41(C7) in the G gamma chain. This was confirmed by DNA sequencing that demonstrated a point mutation at the expected site in exon 2 of the G gamma gene, accounting for the appropriate change in the codon. This substitution, hemoglobin F-Cincinnati, alpha 2 gamma 2 41(C7) Phe-->Ser, not previously described, presumably decreased oxygen affinity of the hemoglobin. This substitution is very near the heme group and the alpha 1 beta 2 interface and, hence, in a crucial area of the globin chain. Abnormalities of gamma globin chains tend to be overlooked due to their transient presence and trivial clinical symptomatology, or due to "in utero" selection when physiologically abnormal. Mutant hemoglobins with altered oxygen affinity should be included in the differential diagnosis of newborns presenting with cyanosis, in whom all common causes have been excluded. -->
ISSN: 1096-8652
0361-8609
DOI: 10.1002/ajh.2830490108
Přístupová URL adresa: https://explore.openaire.eu/search/publication?articleId=doi_________::ea9c4265649b873d7e5521cefa0394b6
https://doi.org/10.1002/ajh.2830490108
Rights: CLOSED
Přírůstkové číslo: edsair.doi...........ea9c4265649b873d7e5521cefa0394b6
Autor: Donald L. Rucknagel, Theodore Zwerdling, Mudra Kohli-Kumar
Rok vydání: 1995
Předmět:
Zdroj: American Journal of Hematology. 49:43-47
ISSN: 1096-8652
0361-8609
DOI: 10.1002/ajh.2830490108
Popis: A term infant presented with mild cyanosis without evidence of hypoxia. Cardiopulmonary disease, polycythemia, and methemoglobinemia were excluded. Standard hemoglobin electrophoresis, including isoelectric focusing, were normal. However, by reverse-phase C4 HPLC, an abnormal globin chain was detected. Analysis of tryptic peptides and amino acid sequence showed that the patient had an amino acid substitution Phe-->Ser at residue 41(C7) in the G gamma chain. This was confirmed by DNA sequencing that demonstrated a point mutation at the expected site in exon 2 of the G gamma gene, accounting for the appropriate change in the codon. This substitution, hemoglobin F-Cincinnati, alpha 2 gamma 2 41(C7) Phe-->Ser, not previously described, presumably decreased oxygen affinity of the hemoglobin. This substitution is very near the heme group and the alpha 1 beta 2 interface and, hence, in a crucial area of the globin chain. Abnormalities of gamma globin chains tend to be overlooked due to their transient presence and trivial clinical symptomatology, or due to "in utero" selection when physiologically abnormal. Mutant hemoglobins with altered oxygen affinity should be included in the differential diagnosis of newborns presenting with cyanosis, in whom all common causes have been excluded.
Databáze: OpenAIRE
Externí odkaz: