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. 2018 Jul 27;13(7):e0197643. doi: 10.1371/journal.pone.0197643

Table 2. Comparison of PEGylation methods for L-asparaginase.

Modification specificitya Modification degree (%)b Activity (%)c Reference
PEG Dichloro-s-triazine (5000 Da) 20–79 45–11 Ashihara et al. [16]
1900 Da 76 20 Ashihara et al. [16]
750 Da 84 16 Ashihara et al. [16]
PEG Vinylpyrrolidone-maleic acid (5000 Da) 33 59 Qian et al. [17]
PEG Succinimidyl succinate (5000 Da) 54 30 Soares et al. [18]
PEG Propionaldehyde (20000 Da) 4 44 Wang et al. [19]
PEG Chloro-s-triazine (10000 Da) 57 11 Matsushima et al. [20]
PEG Chloro-s-triazine (10000 Da) 57 8 Kamisaki et al. [21]
PEG Comb-shaped (100000 Da) 34 86 Kodera et al. [22]
13000 Da 50 46 Kodera et al. [22]
PEG Monosulfone (5000, 10000 & 20000 Da) 4 100 Balan et al. [34]
Dextran-glutaraldehyde 99 35 Balcão et al. [58]
Dimethylsuberimidate 25 17 Handschumacher & Gaumond [59]
PEG Bi-maleimide (5000 Da) 9 130 This work

aModification specificity refers to the functional group in the polymer that is conjugated to L-asparaginase.

bModification degree refers to the average percentage of conjugated sites in comparison to the total amine groups per L-asparaginase tetramer.

cActivity refers to the relative catalytic activity of the bio-PEG-conjugate compared to the non-conjugated L-asparaginase defined as 100% and as reported by each study.