Document Detail

Hemoglobin Shelby [beta 131(H9) Gln----Lys] a correction to the structure of hemoglobin Deaconess and hemoglobin Leslie.
MedLine Citation:
PMID:  6526653     Owner:  NLM     Status:  MEDLINE    
Hemoglobin Shelby, detected in two unrelated black families, has an electrophoretic mobility like Hb F on cellulose acetate (pH 8.4) and a mobility between Hbs S and C on citrate agar (pH 6.2). Globin chain analysis in acid and alkaline buffers revealed an abnormal chain migrating between beta A and beta S. Tests for unstable hemoglobins were positive. Hematologic data on both families indicated carriers have mild anemia. The variant showed a slightly lower affinity for oxygen with normal cooperativity and Bohr effect, and its reactions with 2,3-diphosphoglycerate and inositol hexaphosphate were similar to those of Hb A. Sequence analysis indicated the substitution of lysine for glutamine at position 131 in the beta-chain. In a previous report (1) we described a variant, Hb Deaconess, in which this residue was deleted. On reexamination of the data, we find that Hb Deaconess is identical to Hb Shelby.
W F Moo-Penn; M H Johnson; J E McGuffey; D L Jue
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Publication Detail:
Type:  Case Reports; Journal Article    
Journal Detail:
Title:  Hemoglobin     Volume:  8     ISSN:  0363-0269     ISO Abbreviation:  Hemoglobin     Publication Date:  1984  
Date Detail:
Created Date:  1985-04-10     Completed Date:  1985-04-10     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  7705865     Medline TA:  Hemoglobin     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  583-93     Citation Subset:  IM    
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MeSH Terms
Amino Acid Sequence
Amino Acids / analysis*
Blood Protein Electrophoresis
Chromatography, High Pressure Liquid
Hemoglobins, Abnormal / analysis*
Reg. No./Substance:
0/Amino Acids; 0/Hemoglobins, Abnormal; 56690-69-8/hemoglobin Shelby

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