Comparative studies on cysteine synthase isozymes from spinach leaves.
Three types of cysteine synthase (CSase, EC 4.2.99.8) isozymes were purified from spinach leaves. Each isozyme was isolated to homogeneity by preparative PAGE. These isozymes were revealed to have different primary structures by amino-acid and proteinase digestion analyses, respectively. The enzymes designated as CSase 1, CSase 2 and CSase 3 with reference to the mobility on native PAGE were characterized with respect to physicochemical and enzymatic properties, and it was found that those enzymes had similar properties. It was also found that CSase 1 could be attributed to chloroplasts.
Yamaguchi
T
T
Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University, Japan.
Masada
M
M
D000596:Amino Acids / Q000032:analysis; D002736:Chloroplasts / Q000201:enzymology; D003547:Cysteine Synthase / Q000737:chemistry / Q000302:isolation & purification*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D018724:Spinacia oleracea / Q000201:enzymology*; D014357:Trypsin
D000596:Amino Acids; D007527:Isoenzymes; D003547:Cysteine Synthase; D014357:Trypsin