Arrangement of human erythrocyte membrane proteins
نویسندگان
چکیده
منابع مشابه
Arrangement of human erythrocyte membrane proteins.
The orientation of human erythrocyte membrane protein was examined by enzymic iodination using lactoperoxidase with the glucose-oxidase system for generating peroxide, followed by proteolytic digestion. The outer surface of intact cells was labeled with 125I and the cytoplasmic surface of either resealed ghosts containing lactoperoxidase or of inside-out vesicles was labeled with 131I. Followin...
متن کاملPurification and characterization of transporter proteins from human erythrocyte membrane.
1. Introduction Functions and biochemical properties of several membrane transporter proteins from human erythrocyte, in particular, the glucose transporter (Glut1) and anion exchanger (AE1, also called Band 3) have been extensively characterized. Glut1 is a member of the mammalian facilitative glucose transporter family Glut1-13 (1,2). The 50-kDa integral membrane protein is expressed in all h...
متن کاملNew and old integral proteins of the human erythrocyte membrane.
vitamin B12 binding by transcobalamin II increases risk of neural tube defects. New and old integral proteins of the human erythrocyte membrane Salzer et al, from the University of Vienna, have recently described that vesicles released from Ca ϩϩ /Ca ϩϩ ionophore-treated erythro-cytes are enriched in lipids and proteins that are typically found within lipid microdomains of the parent cell's pla...
متن کاملSite-Specific GlcNAcylation of Human Erythrocyte Proteins
OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity. Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals. RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins or G...
متن کاملPhotoactivated cross-linking of proteins within the erythrocyte membrane core.
We describe the reactions of three lipophilic, photoactivated cross-linking reagents, 1,5-diazidonapthalene, 4,4'-diazidobiphenyl, and the reversible 4,4'-dithiobisphenylazide, with erythrocyte membranes. Cross-linking occurs only upon photoactivation. At pH 7 to 8, only spectrin components are cross-linked by these reagents. At pH 5.0 to 5.5 several additional membrane proteins including the m...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1975
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)41059-4