L-alpha-Hydroxyacid oxidase isozymes. Purification and molecular properties.
L-alpha-Hydroxyacid oxidase isozymes from rat liver (A isozyme) and kidney (B isozyme) have been isolated in a high state of purity with specific activities of 61 and 14.7 microkatals per gram protein respectively. The subunit molecular weights determined by sodium dodecylsulphate polyacrylamide gel electrophoresis were 40000 +/- 3000; the mouse A and B isozymes were also partially purified and their subunit molecular weights shown to be 37000.
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001051:Apoenzymes; D001665:Binding Sites; D005415:Flavins / Q000032:analysis; D006880:Hydroxy Acids; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D009928:Organ Specificity; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet; D013438:Sulfhydryl Compounds / Q000032:analysis
D000596:Amino Acids; D001051:Apoenzymes; D005415:Flavins; D006880:Hydroxy Acids; D007527:Isoenzymes; D013438:Sulfhydryl Compounds; D000429:Alcohol Oxidoreductases