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. 2025 Jun 14;24(7):3412–3428. doi: 10.1021/acs.jproteome.5c00093

3. Reactive Carbonyl Species and Modification Sites Identified in Human Serum Albumin as a Result of Reactive Electrophiles.

Modification Site Distinct Modification Count Modification Mass Shifts Subdomain Lipid-Binding Site
C58 3 +355.131, +369.147, +399.121 IA No
K214 3 +312.089, +369.147, +383.138, +381.147 IIA Site 9
K219 4 +312.089, +383.138, +395.138, +409.142, +457.163, IIA Site 8
K223 11 +312.089, +355.131, +367.131, +369.147, +371.126, +383.138, +385.142, +395.138, +399.121, +409.142, +419.126, +475.174 IIA Site 7/Site 8
K456 2 +312.089, +395.138 IIIA Site 9
K460 1 +395.138 IIIA Site 9
K543 3 +312.089, +383.138, +395.138 IIIB No
K549 6 +355.131, +383.138, +385.142, +395.138, +419.126, +475.174 IIIB Site 5
K565 4 +312.089, + 369.147, + 383.138, + 395.139 IIIB No
K588 1 +355.131 IIIB No
a

Modification site relative to the canonical sequence of HSA (Uniprot ID: P02768).

b

Mass shifts corresponding to unknown ARP-reactive carbonyl species.

c

Based on proximity, no defined electron density to map amino acid orientation.