Table 1. Identified possible substrates for TG1 using pepK5.

Accession number	Name	Days
		0	3	7	14
P05784	Keratin, type I cytoskeletal 18		+	+	+
P24270	Catalase		+	+	+
P62806	Histone H4		+	+	+
P68373	Tubulin α-1C chain		+	+	+
Q8K0E8	Fibrinogen β chain		+	+
Q61781	Keratin, type I cytoskeletal 14		+		+
Q8VDD5	Myosin-9			+	+
Q60597	2-oxoglutarate dehydrogenase, mitochondrial		+
Q9CZX8	40 S ribosomal protein S19		+
P62849	40 S ribosomal protein S24		+
P97351	40 S ribosomal protein S3a		+
P62702	40 S ribosomal protein S4, X isoform		+
Q6ZWV3	60 S ribosomal protein L10		+
P47963	60 S ribosomal protein L13		+
P27659	60 S ribosomal protein L3		+
P56391	Cytochrome c oxidase subunit 6B1		+
Q64459	Cytochrome P450 3A11		+
Q80XN0	D-β-hydroxybutyrate dehydrogenase, mitochondrial		+
Q9DCW4	Electron transfer flavoprotein subunit β		+
Q8VCM7	Fibrinogen γ chain		+
P01942	Hemoglobin subunit α		+
P43274	Histone H1.4		+
Q6GSS7	Histone H2A type 2-A		+
O88844	Isocitrate dehydrogenase [NADP] cytoplasmic		+
Q9QWL7	Keratin, type I cytoskeletal 17		+
Q9WVL0	Maleylacetoacetate isomerase		+
Q91VS7	Microsomal glutathione S-transferase 1		+
Q5SX40	Myosin-1		+
P35700	Peroxiredoxin-1		+
O08709	Peroxiredoxin-6		+
Q80U40	REVERSED RIMS-binding protein 2		+
P05367	Serum amyloid A-2 protein		+
P84104	Splicing factor, arginine/serine-rich 3		+
Q8BMS1	Trifunctional enzyme subunit α, mitochondrial		+
Q9CWF2	Tubulin β-2B chain		+
Q63836	Selenium-binding protein 2		+
Q9Z1T2	REVERSED Thrombospondin-4			+
Q9D2U9	Histone H2B type 3-A				+
Q9D646	Keratin, type I cuticular Ha4				+
Q9Z2K1	Keratin, type I cytoskeletal 16				+
Q9Z2T6	Keratin, type II cuticular Hb5				+
Q921I1	Serotransferrin				+
P68372	Tubulin β-2C chain				+

Liver extract on each indicated day after BDL surgery (n = 3 mice) was incubated with biotinylated pepK5. The peptide-incorporated proteins were then purified using monoavidin gel and subjected to trypsin digestion. The fragmented peptides were fractionated by nano-HPLC and identified using MALDI-TOF/TOF mass spectrometer. The newly identified possible substrates in each indicated day were demonstrated as “+ ” compared to control sample (Day 0). The underlined possible substrates indicate overlapped substrates identified as both peptide (pepK5 and pepT26)-incorporated proteins.