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Table 1 Functionality determination for Cyt c glycoconjugates

From: Chemical glycosylation of cytochrome c improves physical and chemical protein stability

Protein formulation

Glycosylation degree #

Residual activity $(%)

Caspase 3 activation %(%)

Caspase 9 activation %(%)

Degradation rate, K d&(x 10 -2 min -1)

Cyt c

N/A

100

100

100

10.3 ± 0.1

Lac4-Cyt c

4.4 ± 0.4

94 ± 4

95 ± 1

95 ± 9

9.9 ± 0.2

Lac9-Cyt c

9.3 ± 0.2

97 ± 2

86 ± 3

93 ± 8

9.6 ± 0.1

Dex3(1 kD)-Cyt c

3.4 ± 0.9

98 ± 1

91 ± 2

96 ± 4

9.8 ± 0.2

Dex5(10kD)-Cyt c

5.2 ± 0.8

93 ± 4

89 ± 1

94 ± 6

9.5 ± 0.1

Dex8(10kD)-Cyt c

8.3 ± 0.4

95 ± 3

85 ± 2

92 ± 7

9.9 ± 0.3

  1. #Glycosylation degree refers to the number of glycan modified Cyt c lysine residues as determined by 2,4,6-trinitrobenzene sulfonic acid (TNBSA) assay. $The residual activity was calculated with respect to the specific activity of native Cyt c.%The caspase 3 and caspase 9 activation is with respect to the activation induced by non-modified Cyt c. The substrates used for caspase-3 and caspase-9 activation assay were 10 mM DEVD-pNA and 4 mM LEHD-pNA, respectively. &The rate of degradation was calculated for Cyt c and Cyt c glycoconjugates after exposure to 1.5 mM H2O2. Each experiment was performed in triplicate, the values averaged, and the ± values are the calculated SD.