Glycosylation site of band 3, the human erythrocyte anion-exchange protein
- 11 February 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (3) , 554-556
- https://doi.org/10.1021/bi00351a006
Abstract
The band 3 protein has a single glycosylation site on the carboxy-terminal 55 000-dalton tryptic fragment that defines a sequence of the polypeptide on the extracytoplasmic surface of the cell. To locate this site, a novel procedure involving end labeling of the 55 000-dalton tryptic fragment was used. Peptides resulting from partial proteolysis of the end radiolabeled glycoprotein were separated by lectin-Sepharose chromatography and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. The smallest fragment observed defined the distance between the glycosylation site and the amino terminus. The procedure was first tested on a protein for which the location of the glycosylation site is known, HLA-B7 antigen. It was then used to show that the glycosylation site of human band 3 is 28 000 .+-. 3000 daltons from the carboxy terminus of the protein.This publication has 14 references indexed in Scilit:
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