Nucleoside diphosphate kinase from human erythrocytes: purification, molecular mass and subunit structure.
A new procedure for the purification of nucleoside diphosphate kinase from human erythrocytes is described. The enzyme (105 kDa by gel filtration) is made-up of two different kinds of subunits (19.0 and 20.5 kDa), both displaying enzymatic activity. The probable subunit structure of the enzyme is hexameric. The discrepancies related to earlier work are discussed.
Presecan
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E
Institute of Hygiene and Public Health, Cluj-Napoca, Romania.
Vonica
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A
Lascu
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I
D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D008970:Molecular Weight; D009701:Nucleoside-Diphosphate Kinase / Q000302:isolation & purification*; D010770:Phosphotransferases / Q000302:isolation & purification*; D011487:Protein Conformation
D010770:Phosphotransferases; D009701:Nucleoside-Diphosphate Kinase