Erythrocyte membrane skeletal protein bands 4.1 a and b are sequence-related phosphoproteins. 1982

S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak

Bands 4.1 a and b are proteins of 80,000 and 78,000 molecular weight, which are both present at approximately 100,000 copies per erythrocyte ghost. Both proteins are components of the erythrocyte membrane skeleton. Bands 4.1 a and b are labeled when intact erythrocytes are incubated with [32P]orthophosphoric acid, and, therefore, are phosphoproteins. One-dimensional partial proteolytic mapping analysis of 32P-labeled bands 4.1 a and 4.1 b and two-dimensional peptide mapping analysis of 125I-labeled bands 4.1 a and 4.1 b clearly demonstrated that the two proteins are sequence-related phosphoproteins. Band 4.1 purified by standard techniques (Tyler, J. M., Hargreaves, W. R., and Branton, D. (1979) Proc. Natl. Acad. Sci. U. S. A. 76, 5192-5196) contains bands 4.1 a and 4.1 b. Bands 4.1 a and 4.1 b bind to spectrin heterodimers in solution. We conclude that the erythrocyte skeletal proteins bands 4.1 a and 4.1 b are sequence-related phosphoproteins, both capable of binding spectrin.

UI MeSH Term Description Entries
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010750 Phosphoproteins Phosphoprotein
D004589 Electrophoresis, Disc Electrophoresis in which discontinuities in both the voltage and pH gradients are introduced by using buffers of different composition and pH in the different parts of the gel column. The term 'disc' was originally used as an abbreviation for 'discontinuous' referring to the buffers employed, and does not have anything to do with the shape of the separated zones. Electrophoresis, Disk,Disc Electrophoresis,Disk Electrophoresis
D004910 Erythrocyte Membrane The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS. Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts
D004912 Erythrocytes Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN. Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D013049 Spectrin A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane. alpha-Spectrin,beta-Spectrin,alpha Spectrin,beta Spectrin

Related Publications

S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak
January 1984, Progress in clinical and biological research,
S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak
November 1984, Blood,
S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak
January 2006, Folia histochemica et cytobiologica,
S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak
August 1981, The Journal of clinical investigation,
S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak
June 1991, The Journal of biological chemistry,
S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak
June 2005, Anatomical science international,
S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak
July 1980, The Journal of biological chemistry,
S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak
July 1984, Proceedings of the National Academy of Sciences of the United States of America,
S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak
August 2001, Molecular and biochemical parasitology,
S R Goodman, and J Yu, and C F Whitfield, and E N Culp, and E J Posnak
December 1985, The Journal of biological chemistry,
Copied contents to your clipboard!