title: Fatty acylation of a 55 kDa membrane protein of human erythrocytes.
abstract: 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.
authors.affiliation: Department of Chemistry, Bose Institute, Calcutta, India.
authors.forename: A K
authors.initials: AK
authors.lastname: Das
authors.forename: M
authors.initials: M
authors.lastname: Kundu
authors.forename: P
authors.initials: P
authors.lastname: Chakrabarti
authors.forename: J
authors.initials: J
authors.lastname: Basu
mesh_terms: D000215:Acylation; D003429:Cross Reactions; D004912:Erythrocytes / Q000737:chemistry*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification
chemical_list: D008565:Membrane Proteins