HB geelong [β139(H17)ASN → ASP]

Hb Geelong [β139(H17)Asn → Asp] was detected in a German woman of Polish-Russian descent. It is an unstable variant which appears to increase the severity of a (β+ -thalassemic phenotype in the propositus. The electrophoretic properties of Hb A and Hb Geelong are similar on cellulose acetate in both acidic and alkaline conditions. The electrophoretic mobility and the amino acid analysis of βx T-14 indicated the substitution Asn → Asp at β139. The sequence of βXT-14 was confirmed by dansyl-Edman degradation. The slight increase observed in the P50 of whole blood is not intrinsic to the β139 substitution, but is thought to result from an increased 2,3-diphosphoglycerate level in response to anemia. No family studies were possible to investigate the mode of inheritance of either β+ -thalassemia or Hb Geelong in the propositus. Synthetic globin chain ratios suggest that impaired synthesis of the variant globin chain is partially responsible for the low level of Hb Geelong in peripheral blood.

[1]  R. A. Holland,et al.  Oxygen carriage and carbonic anhydrase activity in the blood of a marsupial, the Tammar wallaby (Macropus eugenii), during early development. , 1988, Respiration physiology.

[2]  J. Kister,et al.  Functional properties of hemoglobin in human red cells. I. Oxygen equilibrium curves and DPG binding. , 1987, Respiration physiology.

[3]  R. Carrell,et al.  A Simple Method for the Detection of Unstable Haemoglobins , 1972, British journal of haematology.

[4]  D. Harkness,et al.  The effect of alteration of intracellular 2,3-DPG concentration upon oxygen binding of intact erythrocytes containing normal and mutant hemoglobins. , 1971, Biochemical and biophysical research communications.

[5]  P. Mannucci,et al.  Cellogel electrophoresis of haemoglobins. , 1968, Clinica chimica acta; international journal of clinical chemistry.

[6]  P. Ramwell,et al.  Thin-layer chromatography of 1-dimethylaminonaphthalene-5-sulphonyl derivatives of amino acids present in superfusates of cat cerebral cortex. , 1967, The Biochemical journal.

[7]  J. Clegg,et al.  Abnormal human haemoglobins , 1966 .

[8]  A. Marengo-Rowe.  Rapid electrophoresis and quantitation of haemoglobins on cellulose acetate , 1965, Journal of clinical pathology.

[9]  K. Betke,et al.  Estimation of Small Percentages of Fœtal Hæmoglobin , 1959, Nature.

[10]  A. Mirsky,et al.  PROTEIN COAGULATION AND ITS REVERSAL , 1930, The Journal of general physiology.

[11]  W. Moo-Penn,et al.  Hb Hinsdale [beta 139 (H17)Asn----Lys]: a variant in the central cavity showing reduced affinity for oxygen and 2,3-diphosphoglycerate. , 1989, Hemoglobin.

[12]  D. Sumner,et al.  Hemoglobin Windsor or beta 11 (A8)Val----Asp: a new unstable beta-chain hemoglobin variant producing a hemolytic anemia. , 1989, Hemoglobin.

[13]  H. Wajcman,et al.  Hehoglobin Brest [β127(H5)Gln→LYS] a new Unstable Human Hemoglobin Variant Located at the α1β1 Interface with Specific Electrophoretic Behavior , 1988 .

[14]  L. C. Andrews,et al.  Location of amino acid residues in human deoxy hemoglobin. , 1978, Hemoglobin.

[15]  R. Schneider,et al.  Identification of hemoglobins and hemoglobinopathies by electrophoresis on cellulose acetate plates impregnated with citrate agar. , 1974, Clinical chemistry.

[16]  C. D. de Verdier,et al.  A modified method for the determination of 2,3-diphosphoglycerate in erythrocytes. , 1972, Scandinavian journal of clinical and laboratory investigation.

[17]  J. Beard,et al.  Studies on marsupial proteins. V. Amino acid sequence of the -chain of haemoglobin from the grey kangaroo, Macropus giganteus. , 1971, Australian journal of biological sciences.