Analysis of the spectrin binding domains of globin.
This study describes the results of binding studies between human spectrin and peptides obtained by trypsin digestion of human globin. The globin digest when passed through an affinity column of spectrin-coupled sepharose retained one peptide from both alpha and beta chains of globin. The absorbed peptides were eluted with 4 M guanidine hydrochloride and separated on a reverse phase column by high pressure liquid chromatography. Their amino acid sequence was determined and their position located in the globin molecule.
Bhown
A S
AS
Department of Medicine, University of Alabama, Birmingham 35294.
Hunter
F
F
Bennett
J C
JC
D000595:Amino Acid Sequence; D001665:Binding Sites; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D004912:Erythrocytes / Q000378:metabolism; D005914:Globins / Q000302:isolation & purification / Q000378:metabolism*; D006454:Hemoglobins / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D013049:Spectrin / Q000302:isolation & purification / Q000378:metabolism*; D014357:Trypsin
D006454:Hemoglobins; D010446:Peptide Fragments; D013049:Spectrin; D005914:Globins; D014357:Trypsin