A New Haemoglobin Variant Haemoglobin J Birmingham a 120 (H3) Ala → Glu

Abstract

An abnormal haemoglobin, which on paper electrophoresis has the mobility of Hb J, has been found in two brothers and, in the heterozygousstate at least, is not associated with serious clinical abnormality. The structure of this hitherto unreported haemoglobin is a 120(H3) Ala -+ Glu and it is named Haemoglobin J Birmingham.A fast moving haemoglobin whose electrophoretic mobility on paper at pH 8.6 was similar to that of HbJ, was discovered in two brothers from Bangladesh during a pilot study of abnormal haemoglobins in immigrant Birmingham schoolchildren. This component appeared to represent approximately 20% of the total haemoglobin. MATERIAL AND METHODSThe initial screening for abnormal haemoglobins was performed on capillary blood samples as previously described by Stuart, Schwartz, Little and Raine (1973). On detection of the abnormal haemoglobin, the boys were asked to attend Birmingham Children's Hospital for clinical examination and further haematological investigations, which followed standard methods (Dacie and Lewis, 1968).Blood was haemolysed as previously described (Lehmann and Huntsman, 1974). Electrophoresis of the haemolysate was done on paper in Tris-buffer, pH 8.9 (Cradock-Watson et aI., 1959) and on starch gel, pH 8.3 (Smithies, 1959).For structural studies, the haemolysate was chrornatographed on a DEAE Sephadex A-50 column (Huisman and Dozy, 1965) at 4°C, using a linear gradient pH 8.2-7.2 (Tris-HCI buffer) to isolate the HbJ. All fractions were concentrated by ultrafiltration using a Sartorius Collodion bag.Haem was removed by 1.5 % HCI-acetone precipitation at -20°C (Rossi-Fanneli et al., 1958) and the precipitated globin washed four times with acetone at -20°C, to remove HCI, then dried under nitrogen. The abnormal ex chain was isolated using a minor modification of the procedure of Clegg, Naughton and Weatherall (1966) and then dialysed against 0.5 % formic acid and Iyophilised.By methods described previously (Lehmann and Huntsman, 1974;Sick et al., 1967), the abnormal o-chain was digested with trypsin (TPCK treated, Worthington Biochemicals Corp., N.J.) and twodimensional paper chromatograms (fingerprints) prepared for diagnostic and preparative purposes. The insoluble tryptic peptides were digested with pepsin and fingerprints prepared (Lorkin et al., 1970.) Peptides on fingerprints were identified by staining either with ninhydrin, 0.2 g/IOO ml (for diagnostic fingerprints), or ninhydrin, 0.02 g/IOO ml (for preparative fingerprints). The diagnostic fingerprints were further stained for sulphur

Hb J Meerut, a fast‐moving hemoglobin—a study of seven cases from India and a review of literature

“…Hb J Meerut/Hb Birmingham is a a-globin chain derived FMH characterized by replacement of alanine by glutamate at 120 amino acid position (a 120 Ala-Glu). Blackwell et al first reported this Hb variant in two sisters from Meerut, India [4], and Kamuzora et al reported in two brothers from Bangladesh [5] Harano et al [6] and Takemura et al [7] reported this Hb variant in two unrelated Japanese families; and Yalcin et al (1994) [1] in a family from Turkey. Our study is the largest reported series of Hb J Meerut of which four patients belonged to one family.…”

Hb J- Meerut [α 120 (H3) Ala ->Glu (α1)] In A Turkish Male

“…Hb J-Meerut results from a C ->A mutation (GCG->GAG) at codon 120 of the α1 or α2 globin gene, changing the alanine to glutamic acid at residue 120 of the α chain 1 , 2 , 3 . This variant was first reported in two sisters from Meerut, Utlar Pradesh, India 1 and in two brothers from Bangladesh living in Birmingham, England 2 ; subsequently the same abnormal hemoglobin, was described in one Japanese family 4 and in one Turkish family 5 . The present study provides details about α Hb J Meerut heterozygous Turkish male who is unrelated to the family with the same abnormal hemoglobin described previously from Turkey.…”