The separation, prtial purificatio nd some properties of isoenzymes of aldolase from XXXX cerebral cortex.

@entity4859 @entity3793 @entity840 @entity39157 @entity4567 @entity376
1. Aldolase isoenzymes from @entity840 cerebral cortex were partially purified and separated by @entity4859 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 @entity3793 and @entity376 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 ( @entity4567 / @entity39157 ) were measured and all were in the range 12-44.
