PURIFICATION OF A 28 KD NON-AGGREGATING TRYPTIC PEPTIDE OF THE DUFFY BLOOD-GROUP PROTEIN

被引:17
作者
WASNIOWSKA, K [1 ]
EICHENBERGER, P [1 ]
KUGELE, F [1 ]
HADLEY, TJ [1 ]
机构
[1] LOUISVILLE AMER RED CROSS,LOUISVILLE,KY 40292
关键词
D O I
10.1006/bbrc.1993.1424
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Duffy blood group aritigenic epitopes are located on a 35-43 kD integral membrane protein of the erythrocyte membrane. This protein functions as a receptor for the human malaria parasite, Plasmodium vivax. The Duffy protein has been difficult to purify because of its tendency to form aggregates. Here we describe purification of a 28 kD tryptic fragment of the Duffy protein and purification of an 18 kD de-glycosylated form of the Duffy tryptic peptide using Thiopropyl Sepharose 6B chromatography and preparative SDS-PAGE. These Duffy-reactive peptides do not form aggregates and may prove amenable to protein sequencing. © 1993 Academic Press.
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收藏
页码:366 / 372
页数:7
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