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. 1979 Jun 29;48(1):1-12.
doi: 10.1007/BF01869253.

Proteolytic degradation of human erythrocyte band 3 by membrane-associated protease activity

G Tarone, N Hamasaki, M Fukuda, V T Marchesi

Proteolytic degradation of human erythrocyte band 3 by membrane-associated protease activity

G Tarone et al. J Membr Biol. .

Abstract

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 were incubated in the cold; this process was greatly accelerated by incubating ghosts at 37 degrees 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 degrees for prolonged periods. These results suggest that human erythrocytes contain tightly bound, membrane-associated proteolytic activity.

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