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Nucleoside diphosphate kinase from human erythrocytes: Purification, molecular mass and subunit structure
Author(s) -
Presecan Elena,
Vonica Alin,
Lascu Ioan
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80811-7
Subject(s) - protein subunit , enzyme , biochemistry , size exclusion chromatography , molecular mass , nucleoside , chemistry , nucleoside diphosphate kinase , kinase , microbiology and biotechnology , biology , gene
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.

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