Phosphatidylinositol 4-phosphate kinase is associated with the membrane skeleton in human erythrocytes.
Phosphatidylinositol 4-phosphate kinase was eluted from human erythrocyte stroma by three separate and distinct techniques which are known to disrupt the membrane skeleton. In addition, this kinase was found to be associated with the intact skeletons prepared by Triton X-100 extraction of stroma. Phosphatidylinositol 4-phosphate kinase which has been extracted from the membrane is a freely soluble protein with poor enzymatic activity toward added phosphatidylinositol-4-phosphate; however, the enzyme was shown to reassociate with skeleton-depleted stroma and then regain full enzymatic activity toward stromal bound substrate.
D004910:Erythrocyte Membrane / Q000201:enzymology*; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis; D010770:Phosphotransferases / Q000097:blood*; D017853:Phosphotransferases (Alcohol Group Acceptor); D012995:Solubility
D008565:Membrane Proteins; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C020077:1-phosphatidylinositol-4-phosphate 5-kinase