Complexes containing actin and spectrin from erythrocyte and brain. 1983

D C Lin, and M D Flanagan, and S Lin

A complex of proteins with properties similar to those of erythrocyte spectrin-band 4.1-actin complex has been identified in a preparation derived from bovine brain. The complex has an apparent sedimentation coefficient of about 26S, and contains brain spectrin (also called fodrin) and actin as major components. The actin in the complex is in the oligomeric form, which nucleates assembly of actin filaments that grow from the "barbed" end. The complex cross-links actin filaments, resulting in an increase in low-shear viscosity. Whether the complex contains a protein analogous to erythrocyte band 4.1 is not known. However, it can be demonstrated that brain spectrin has the capability to interact with band 4.1 in a way which increases its ability to cross-link actin filaments.

UI MeSH Term Description Entries
D001923 Brain Chemistry Changes in the amounts of various chemicals (neurotransmitters, receptors, enzymes, and other metabolites) specific to the area of the central nervous system contained within the head. These are monitored over time, during sensory stimulation, or under different disease states. Chemistry, Brain,Brain Chemistries,Chemistries, Brain
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
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
D000199 Actins Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle. F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
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

D C Lin, and M D Flanagan, and S Lin
January 1978, Journal of supramolecular structure,
D C Lin, and M D Flanagan, and S Lin
January 1987, Australian journal of biological sciences,
D C Lin, and M D Flanagan, and S Lin
January 1989, Biochimica et biophysica acta,
D C Lin, and M D Flanagan, and S Lin
January 1987, Nature,
D C Lin, and M D Flanagan, and S Lin
March 1987, FEBS letters,
D C Lin, and M D Flanagan, and S Lin
October 1983, The Journal of cell biology,
D C Lin, and M D Flanagan, and S Lin
January 1996, Journal of biochemistry,
D C Lin, and M D Flanagan, and S Lin
November 1978, Biochimica et biophysica acta,
Copied contents to your clipboard!