Table 2.

Supplementary Ub Is Not Required for Stimulation of α-Chain Degradation by Ubal

Lysate DonorUb AddedDegradation of 3H-α-ChainsUbal-Promoted
(μmol/L)No Ubal0.6-0.8 μmol/L UbalIncrease (%)
S.O. 9.3 11.2 20.9 
 47 10.3 12.7 23.7 
C.G. 3.8 12.1 219.2 
 47 7.2 13.9 92.6 
P.C. 6.6 10.5 58.5 
 47 8.6 11.6 35.8 
S.D. 4.8 6.9 43.2 
 47 6.4 7.7 20.1 
Lysate DonorUb AddedDegradation of 3H-α-ChainsUbal-Promoted
(μmol/L)No Ubal0.6-0.8 μmol/L UbalIncrease (%)
S.O. 9.3 11.2 20.9 
 47 10.3 12.7 23.7 
C.G. 3.8 12.1 219.2 
 47 7.2 13.9 92.6 
P.C. 6.6 10.5 58.5 
 47 8.6 11.6 35.8 
S.D. 4.8 6.9 43.2 
 47 6.4 7.7 20.1 

Each reaction mixture was prepared with a dialyzed hemolysate from the blood cells of 1 of 4 β-thalassemic donors, 3H-α-chains as substrate, ATP, and an ATP-regenerating system with or without the usual concentration (47 μmol/L) of supplementary Ub. Replicate mixtures contained 0 to 1.0 μmol/L Ubal and were incubated at 37°C for 2 hours. Curves of ATP-dependent proteolysis similar to those shown in Fig 2 were plotted after subtraction of ATP-independent degradation values of 2.1%, 2.5%, 1.3%, and 1.8% obtained with the lysates from S.O., C.G., P.C., and S.D., respectively. Values for ATP-dependent proteolysis (% TCA-soluble radioactivity) of 3H-α-chains from mixtures without Ubal and from those with a Ubal concentration (0.6 to 0.8 μmol/L) resulting in maximum stimulation of degradation together with the corresponding calculated % increase are presented.

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