The separation, prtial purificatio nd some properties of isoenzymes of aldolase from guinea-pig cerebral cortex.
1. Aldolase isoenzymes from guinea-pig cerebral cortex were partially purified and separated by ammonium sulphate fractionation and chromatography on DEAE-cellulose. 2. Each purified isoenzyme was shown to be virtually uncontaminated with other forms by starch-gel electrophoresis. The quantitative distribution of the isoenzymes was: I, 6.2%; II, 5.2%; III, 15.3%; IV, 25.7%; V, 33.3%. 3. The pH optima for the five separated isoenzymes were similar; all were in the range pH7.5-8.0. Values for pK(a) (6.31-6.55) and pK(b) (9.45-9.59) were calculated from the data and suggested the involvement of histidine and lysine residues. 4. The stabilities of the isoenzymes were shown to be I=II>III>IV>V at pH4.4 in order of decreasing stability and are discussed in terms of subunit structure. 5. The substrate activity ratios (fructose 1,6-diphosphate/fructose 1-phosphate) were measured and all were in the range 12-44.
D000818:Animals; D002021:Buffers; D002482:Cellulose; D002540:Cerebral Cortex / Q000201:enzymology*; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002621:Chemistry; D002852:Chromatography, Ion Exchange; D004355:Drug Stability; D004586:Electrophoresis; D005634:Fructose-Bisphosphate Aldolase / Q000032:analysis / Q000302:isolation & purification; D005782:Gels; D006168:Guinea Pigs; D006600:Hexosephosphates; D006639:Histidine; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000032:analysis / Q000302:isolation & purification; D008239:Lysine; D008722:Methods; D000644:Quaternary Ammonium Compounds; D012995:Solubility; D013213:Starch; D013997:Time Factors; D014461:Ultracentrifugation
D002021:Buffers; D005782:Gels; D006600:Hexosephosphates; D007527:Isoenzymes; D000644:Quaternary Ammonium Compounds; D006639:Histidine; D002482:Cellulose; D013213:Starch; D005634:Fructose-Bisphosphate Aldolase; D008239:Lysine
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