The Characterization of Hemoglobin Shimonoseki-Reference-Cited by-同舟云学术

The Characterization of Hemoglobin Shimonoseki

Published:1964-11-01 Issue:5 Volume:24 Page:624-635
ISSN:0006-4971
Container-title:Blood
language:en
Short-container-title:

Author:

HANADA M.¹²,RUCKNAGEL D. L.¹¹

Affiliation:

1. Department of Human Genetics, University of Michigan Medical School, Ann Arbor, Mich.

2. Department of Human Genetics, University of Michigan Medical School, Ann Arbor, Mich.; Present Address: First Department of Internal Medicine, University of Kyushu Medical School, Fukuoka, Japan

Abstract

Abstract Hemoglobin Shimonoseki, discovered in western Japan in 1960, has been further characterized as a mutant with abnormal α-polypeptide chains on the basis of: (1) The presence of a minor hemoglobin component migrating cathodally at pH 8.6 to Hb A2, presumably α2Shσ2A2. (2) Hybridization studies. (3) Fingerprinting of isolated α-polypeptide chains. Hemoglobin Sh is characterized by the substitution of arginine for glutamine at residue 54 and can therefore be designated as α254Argβ2A.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

Link

http://ashpublications.org/blood/article-pdf/24/5/624/572066/624.pdf

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