J. Desneves et al., HUMAN ERYTHROCYTE BAND 7.2B IS PREFERENTIALLY LABELED BY A PHOTOREACTIVE PHOSPHOLIPID, Biochemical and biophysical research communications, 224(1), 1996, pp. 108-114
A head-group modified, photoreactive analog of phosphatidylethanolamin
e, 1,2-dilauryl-sn-glycero-3-phosphatidylethanolamine ([I-125]-N-ASA-D
LPE). has been used in photoaffinity labeling studies of proteins of t
he human erythrocyte membrane. [I-125]-N-ASA-DLPE was shown to be pref
erentially incorporated into a protein with an apparent molecular weig
ht of 31 kDa. protein sequencing and immunoprecipitation were used to
identify this protein as the erythrocyte membrane protein, and 7.2b or
stomatin. A sulphydryl-reactive ligand, -N-[2-(2-pyridinyldithio)ethy
l]-benzenepropanamide ([I-125]-PDA), was also shown to preferentially
label band 7.2b, We propose that band 7.2b may act as a site of transb
ilayer reorientation of membrane phospholipids. (C) 1996 Academic Pres
s, Inc.