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Purification and partial characterization of spinach leaf glycerate kinase
Author(s) -
Kleczkowski Leszek A.,
Randall Douglas D.
Publication year - 1983
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(83)80603-6
Subject(s) - spinach , fractionation , enzyme , chemistry , monomer , biochemistry , photosynthesis , affinity chromatography , chromatography , pi , peg ratio , organic chemistry , finance , economics , polymer
Glycerate kinase from spinach leaves was purified to near homogeneity using PEG/MgCl 2 fractionation, ion exchange, molecular sieving and affinity chromatography. The purified enzyme is a monomer of M r 40 000, shows a pI‐value of 4.8 and a broad pH optimum of 6.5–8.5 and is specific for D‐isomer of glycerate. The high activity of crude enzyme (≈ 150 μmol. h −1 .mg chl −1 ) indicates that glycerate kinase does not limit the oxidative photosynthetic carbon cycle.