Human erythrocyte ankyrin. Purification and properties.
نویسندگان
چکیده
منابع مشابه
Purification and properties of human erythrocyte carbonic anhydrases.
Three different methods are described for separating hemoglobins from carbonic anhydrases in hemolysates from human erythrocytes. The preferred method involves adsorption on diethylaminoethyl Sephadex at pH 8.7 followed by selective elution of the carbonic anhydrases. Carbonic anhydrases A, B, and C are subsequently separated from each other on DEAE-Sephadex by elution with 0.05 M Trischloride ...
متن کاملPurification and properties of human erythrocyte glutathione peroxidase.
Glutathione peroxidase has been purified to homogeneity from human erythrocytes. The purification steps involved ammonium sulfate precipitation of hemolysate, CM-cellulose (CM-52), DEAE-cellulose (DE52), Sephadex G-200, and DEAE-Sephadex column chromatography. In the last step, i.e. DEAE-Sephadex A-25 column chromatography, the enzyme was eluted in a major peak and tailing fraction. The major p...
متن کاملcDNA sequence for human erythrocyte ankyrin.
The cDNA for human erythrocyte ankyrin has been isolated from a series of overlapping clones obtained from a reticulocyte cDNA library. The composite cDNA sequence has a large open reading frame of 5636 base pairs (bp) with the complete coding sequence for a polypeptide of 1879 amino acids with a predicted molecular mass of 206 kDa. The derived amino acid sequence contained 194 residues that we...
متن کاملHuman erythrocyte myosin: identification and purification
Human erythrocytes contain an Mr 200,000 polypeptide that cross-reacts specifically with affinity-purified antibodies to the Mr 200,000 heavy chain of human platelet myosin. Immunofluorescence staining of formaldehyde-fixed erythrocytes demonstrated that the immunoreactive myosin polypeptide is present in all cells and is localized in a punctate pattern throughout the cell. Between 20-40% of th...
متن کاملPurification of Human Erythrocyte Pyruvate ICinase*
We describe a purification scheme for human erythrocyte pyruvate kinase. Following two ammonium sulfate fractionations, batchwise absorption on CM-cellulose, chromatography on CM-cellulose with fructose 1,6-diphosphate elution, and chromatography on DEAE-cellulose, a 30,000fold purification was achieved with a yield of 8% from the original hemolysate. Antiserum against partially purified pyruva...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85926-4