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. 1999 Mar;119(3):979–988. doi: 10.1104/pp.119.3.979

Table I.

Purification scheme for the acidic form and alkaline forms I and II α-galactosidases from C. melo fruit

Purification Step Enzyme Activity Protein Specific Activity Recovery Purification
units mg units × 10 mg−1 protein % -fold
Acid form
 Crude extract 13.0 1152 0.11 100
 5% to 50% PEG fraction 11.4 481 0.24 88 2
 DEAE-Sepharose 4.6 45 1.02 35 9
 Sephadex-200 3.0 13 2.32 23 21
 ConA 1.7 2.6 6.27 13 55
Alkaline form I
 Crude extract 27.7 1152 0.24 100
 5% to 50% PEG fraction 20.7 481 0.43 75 2
 DEAE-Sepharose 9.5 35 2.73 34 11
 Mono-Q 8.0 15 5.37 29 22
 Bio-gel HTP 5.1 3.7 13.82 19 57
Alkaline form II
 Crude extract 18.4 1152 0.16 100
 5% to 50% PEG fraction 16.4 481 0.34 89 2
 DEAE-Sepharose 10.9 58 1.89 59 12
 Mono-Q 8.8 17 5.21 48 33
 Phenyl Sepharose 6 fast flow 5.8 2.9 19.73 31 123

All specific activities were assayed using raffinose (for acid and alkaline form I) or stachyose (for alkaline form II) as the substrate.