[Primary structure of bovine erythrocyte carbonic anhydrase CI. I. Tryptic peptides].
Bovine erythrocyte carbonic anhydrase CI consists of 259 amino acid residues including 18 lysines and 9 arginines. Its primary structure has been first investigated by isolation and sequence determination of the tryptic units. Acidification of the tryptic hydrolysate leads to the precipitation of 40% of the peptidic material. All the acid soluble peptides were isolated from the supernatant by chromatography on Dowex 50 W-X2 and Dowex 1-X2 followed by purification of heterogeneous fractions. Two of the three  acid insoluble peptides were obtained in a pure form from the whole tryptic hydrolysate by gel filtration on Sephadex G-50 and chromatography on DEAE-Sephadex in alkaline medium. The sequence of the so isolated tryptic units has been determined with the exception of two of them obtained in a very poor yield.
D000595:Amino Acid Sequence; D000818:Animals; D002256:Carbonic Anhydrases / Q000097:blood*; D002417:Cattle; D004912:Erythrocytes / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D010446:Peptide Fragments / Q000302:isolation & purification; D012995:Solubility; D014357:Trypsin
D010446:Peptide Fragments; D014357:Trypsin; D002256:Carbonic Anhydrases
Structure primaire de l'anhydrase carbonique érythrocytaire bovine CI. I. Peptides trypsiques