Fatty acylation of a 55 kDa membrane protein of human erythrocytes.
The major palmitoylated human erythrocyte membrane protein has an M(r) of 55,000. It is distinct from the glucose transporter and is not derived from band 3 or ankyrin. It resists salt extraction suggesting a high affinity for the membrane. Pulse chase experiments demonstrate that palmitoylation is a dynamic process, and it may therefore have regulatory significance in membrane protein-protein or protein-lipid interaction. Slower dynamics of palmitoylation in erythrocytes from patients suffering from chronic myelogenous leukemia, which are less stable than normal erythrocytes, strengthen this view.
Das
A K
AK
Department of Chemistry, Bose Institute, Calcutta, India.
Kundu
M
M
Chakrabarti
P
P
Basu
J
J
D000215:Acylation; D003429:Cross Reactions; D004912:Erythrocytes / Q000737:chemistry*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification
D008565:Membrane Proteins