| Literature DB >> 3021063 |
Abstract
Adenylate kinase from human erythrocytes and skeletal muscle can be purified to homogeneity by a new procedure based on DEAE-Sepharose and Blue Sepharose affinity chromatography and Sephadex G-75 fractionation. For the enzyme purified from erythrocytes the specific activity is 3,000 U/mg of protein, and the overall yield is 70%. For the enzyme purified from skeletal muscle the specific activity is 2,075 U/mg of protein, and the overall yield is 44%. The sequence of steps takes advantage of the high isoelectric point, the high affinity for Blue Sepharose, and the low molecular weight of the isoenzyme from these two human tissues.Entities:
Mesh:
Substances:
Year: 1986 PMID: 3021063 DOI: 10.1016/0003-9861(86)90696-x
Source DB: PubMed Journal: Arch Biochem Biophys ISSN: 0003-9861 Impact factor: 4.013