PROTEOLYTIC DEGRADATION OF HUMAN-ERYTHROCYTE BAND-3 BY MEMBRANE-ASSOCIATED PROTEASE ACTIVITY

被引:57
作者
TARONE, G [1 ]
HAMASAKI, N [1 ]
FUKUDA, M [1 ]
MARCHESI, VT [1 ]
机构
[1] YALE UNIV,SCH MED,DEPT PATHOL,NEW HAVEN,CT 06510
关键词
D O I
10.1007/BF01869253
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
Antisera directed against the cytoplasmic portion of human erythrocyte Band 3 were used to follow the degradation of the band 3 molecule. Small amounts of Band 3 were degraded when well-washed red cell membrane ghosts were incubated in the cold; this process was greatly accelerated by incubating ghosts at 37°C. Band 3 labeled with pyridoxal-phosphate was digested at comparable rates. Band 3 digestion also took place when alkali-extracted ghost membranes were incubated at 37° for prolonged periods. These results suggest that human erythrocytes contain tightly bound, membrane-associated proteolytic activity. © 1979 Springer-Verlag New York Inc.
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页码:1 / 12
页数:12
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