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African Journal of Pig Farming ISSN 2375-0731 Vol. 5 (12), pp. 001-006, December, 2017. Available online at 
www.internationalscholarsjournals.org © International Scholars Journals 

 

Author(s) retain the copyright of this article. 

 
 

Full Length Research Paper 

 

Comparative proteomic analysis of the effects of dietary 
mugwort (Artemisia iwayomogi Kitamura) on the pig 

Longissimus dorsi muscle 

 
Byung Uk Kim1, Mi Ae Jeong1, Yeon Sun Ryu2, Hwa Chun Park 3, Jong Hyun Jung3, Sam 

Woong Kim4, Chul Wook Kim1, Young Min Song1, Ki Hwa Chung1, Il Suk Kim1, Sang Keun 
Jin1, Sang Suk Lee5, In Soon Choi6 and Kwang Keun Cho1* 

 
1
Department of Animal Resources Technology, Gyeongnam National University of Science and Technology, 150 Chilam- 

dong, Jinju, Gyeongnam, 660-758, Republic of Korea. 
2
Department of Animal Health Management, Woosuk University, 443 Samnye-eup, Wanju-gun, Jeonbuk, 565-701, 

Republic of Korea. 
3
Dasan Genetics, Gasan-ri, Unbong-ub, Namwon-city Jeonbuk, Republic of Korea. 

4
Swine Science and Technology Center, Gyeongnam National University of Science and Technology, 150 Chilam-dong, 

Jinju, Gyeongnam, 660-758, Republic of Korea. 
5
Department of Animal Science and Technology, Sunchon National University, Suncheon 540-742, Republic of Korea. 

6
Department of Biological Sciences, Silla University, Busan, 617-736, Republic of Korea. 

 
Accepted 03 August, 2017 

 
Proteomic analysis by 2-dimensional electrophoresis (2-DE) of the longissimus dorsi muscle in finishing pigs (LY × D) 
grown on a diet supplemented with mugwort powder found roughly 300 spots on a polyacrylamide gel image. Among 
them, the expression levels of 12 spots were higher than those of the control group. From the results of peptide mass 
fingerprinting (PMF) analysis, nine proteins were characterized: myosin light chain 2V, elF-5A, myosin light chain 1, F1-
ATPase chain D, peroxiredoxin-2, Kelch-related protein 1, SLA-7, glycine amidinotransferase, and Tpi 1. The other three 
spots with increased expression were identified by chemically assisted fragmentation-matrix-assisted laser 
desorption/ionization (CAF-MALDI) sequencing as serum albumin precursor and two different types of myoglobin. 
Taken together, these results indicate that mugwort powder has the potential to improve the quality of pork meat. 

 

Key words: 2-DE, longissimus dorsi muscle, meat quality, mugwort, pig, proteome. 

 
INTRODUCTION 

 
Because proteins play critical roles in transport, immune 
responses, storage, and structure, and serve as 
members of metabolic pathways, they are essential 
factors for the maintenance of life of all organisms. Thus, 
proteomic tools were developed to investigate overall 
protein expression patterns (Anderson and Anderson, 
1998; Blackstock and Weir, 1999; Wilkins et al., 1996). 
From 2-DE-based-proteomic analysis of proteins from 
white and red pork muscles, about 500 spots were 
obtained, and five spots were observed with different  
 

 
*Corresponding author. E-mail: chotwo2@gntech.ac.kr. Tel: 82- 
55-751-3286. Fax: 82-55-751-3280. 

 
 
 

 
expression patterns including myoglobin, two slow-twitch 
isoforms of myosin light chain, and two small heat shock 
proteins (Kim et al., 2004).  

Oriental medicines have antibiotic, anti-cancer, anti-
oxidant, and physiological activation properties, and there 
is a trend towards their increased utilization as feed 
additives because of the potential for improving intestinal 
microbiota as well as pig meat quality. In particular, 
mugwort grows naturally everywhere in South Korea, so it 
may be an invaluable feed additive. The major 
components of mugwort are alkaloids, essential oils, 
vitamins, and various minerals (Kang et al., 1995), and its 
pharmacological properties include anti-oxidative (Lee et 
al., 1992; Sim et al., 1992), anti-cancer (Lim and Lee, 



 
 
 

 

1997; Sun et al., 1992), and liver protective activities 
(Gilanti et al., 2005). Pigs fed mugwort powder improved 
their average weight gain, protein content, and the 
lightness of their meat and fat (Kim et al., 2008).  

The improvement of pig meat quality through a 
mugwort powder diet should be accompanied by altered 
expression of the relevant genes. Therefore, this study 
used comparative 2-DE to investigate global changes in  
protein expression in longissimus dorsi muscle 

associated with dietary mugwort supplementation. 
 

 
MATERIALS AND METHODS 
 
Experimental animals and sample harvesting 
 
Experimental diets included a control diet (C group), and a diet 
supplemented with 1.5% (w/w) mugwort powder as a diet additive 
(T group). Among 20 selected growing landrace (LYxD) pigs of  
body weight 75  4 kg, half were grown for 50 days on the basal 
diet, whereas the other half was grown on the mugwort powder diet. 
Longissimus dorsi muscle tissues of the carcass were harvested 
from four pigs that exhibited good breeding in each group, and 
these were then used for the experiment. 

 

Protein extraction from Longissimus dorsi muscle 
 
The harvested Longissimus dorsi muscle tissues were sonicated for 
10 s with a Sonoplus (Bandelin electronic, Germany) and were then 
directly homogenized by a motor-driven homogenizer 
(PowerGen125, Fisher Scientific) in sample lysis solution composed 
of 7 M urea, 2 M thiourea, 4% (w/v) 3 - [(3 -cholamidopropy) 
dimethyammonio]- 1 - propanesulfonate (CHAPS), 1% (w/v) 
dithiothreitol (DTT), 2% (v/v) pharmalyte, and 1 mM benzamidine. 
After the homogenized product was centrifuged at 15,000 × g for 1 
h at 15°C, the precipitated insoluble material was discarded, and a 
soluble supernatant fraction was collected and used for 2-DE. 
Protein quantity for sample loading was normalized by Bradford 
assay (Bradford, 1976). 

 

Protein separation via 2-DE and analysis of gel images 
 
Immobilized pH gradient (IPG) dry strips were equilibrated for 12 to 
16 h with equilibration buffer (7 M urea, 2 M thiourea, 2% CHAPS, 
1% DTT, and 1% pharmalyte), and 1.1 mg of each sample was 
loaded onto a strip fixed in a strip module. Isoelectric focusing (IEF) 
was performed at 20°C using a Multiphor II electrophoresis unit and 
an EPS 3500 XL power supply (Amersham Biosciences) according 
to the manufacturer’s instruction. The voltage for IEF was linearly 
increased from 150 to 3,500 V over 3 h for sample entry into the gel 
followed by constant 3,500 V for complete focusing until 96 kV/h. 
Prior to electrophoresis in the second dimension, the treated strips 
were incubated for 10 min each in equilibration buffer (50 mM Tris-
Cl, pH 6.8, 6 M urea, 2% SDS and 30% glycerol) plus 1% DTT and 
then equilibration buffer plus 2.5% iodoacetamide. The equilibrated 
strips were inserted into SDS-PAGE gels (20 × 24 cm, 10 - 16%). 
Protein separation via SDS-PAGE was performed with a Hoefer 
DALT 2D system (Amersham Biosciences) according to the 
manufacturer’s instructions. 2-DE gels were run for 1,700 V/h at 
20°C and then were stained with Coomassie brilliant blue G250 
solution as described by Anderson et al. (1991). Colloidal CBB 
staining of 2-DE gels was used to delicately analyze the protein 
spots, and the solution was prepared with 177 ml 85% phosphoric 
acid, 150 g ammonium sulfate, 1. 8 g CBB-G 250, adjusted to 1,200 

 
 
 
 

 
ml with water, and then finally adjusted to 1,500 ml with methanol. 

Quantitative analysis of digitized gel images was carried out  
using the PDQuest software (version 7.0, Bio-Rad) according to the 
protocols provided by the manufacturer. The quantity of each spot 
was normalized by total valid spot intensity. Protein spots showing 
significant expression variation were selected as spots to exhibit 
critical changes between the control and treated groups. 

 

Protein identification via PMF and CAF-MALDI sequencing 
 
Protein identification via PMF was done as follows: protein spots 
were enzymatically digested with modified porcine trypsin in a 
manner similar to the method previously described by Shevchenko 
et al. (1996). Target spots were cut from separated gels by 2-DE. 
The gel pieces were washed with 50% acetonitrile to remove SDS, 
salt, and staining dye, dried to remove solvent, rehydrated with 

trypsin solution (8 to 10 ng/L), and then incubated for 8 to 10 h at  
37°C. The proteolytic reaction was terminated by addition of 5 l 
0.5% trifluoroacetic acid (TFA). Tryptic peptides were recovered by 
combining the aqueous phases obtained from several extractions of 
gel pieces with 50% aqueous acetonitrile. After concentration, the 
peptide mixture was desalted using C18ZipTips (Millipore), and  
peptides were eluted in 1 to 5 lacetonitrile. An aliquot of this 
solution was mixed with an equal volume of a saturated solution of 
α-cyano-4-hydroxycinnamic acid in 50% aqueous acetonitrile, and 1  
l of the mixture was spotted onto a target plate. 

Protein analysis via PMF was performed by an Ettan matrix-
assisted laser desorption/ionization-time of flight (MALDI-TOF; 
Amersham Biosciences). Peptides were evaporated with an N2 
laser at 337 nm, and a delayed extraction approach was used. They 
were accelerated with a 20-kV injection pulse for time of flight 
analysis. Each spectrum is the cumulative average of 300 laser 
shots. The search program profound, which was developed by the  
Rockefeller University (http://129.85.19.192/profound_bin/ 
WebProFound.exe), was used for protein identification by PMF. 
Spectra were calibrated with trypsin auto-digestion ion peaks m/z 
842.510 and 2211.1046 as internal standards.  

CAF-MALDI sequencing was done by the following method 
described here briefly. Protein digestion was performed by the 
same method as with PMF described above. 4-sulfophenyl-
isothiocyanate (SPITC, Aldrich) reaction was done by the procedure 
of Dongxia et al. (2004). A total of 10 mg/ml (final) SPITC was 
dissolved in 20 mM NaHCO3, pH 9.5 and then treated with a half 
volume of SPITC solution versus one volume of trypsin-digested 
solution. The reaction continued for 30 min at 55°C and was then  
terminated by adding 1 l 5% TFA. The subsequent procedures 
were performed via the same method as was used for PMF. 

 

Statistical analysis 
 
Statistical analysis was done by general linear model (GLM) 
method of the SAS Program (Statistics Analytical System, USA, 
1999). Duncan's multiple range tests was used to compare the 
differences between the means of the investigated samples. The 

results of the statistical analysis are presented as mean  standard 
deviation (SD). 
 
 
RESULTS AND DISCUSSION 

 
Changes in protein expression patterns by mugwort 
powder 
 
Mugwort powder contains various physiologically active 
materials, and the tissue of animals fed with the powder 



   
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 

Figure 1. Full 2-DE gel image of proteins from the Longissimus dorsi muscle of pigs fed with mugwort 
powder. The 1st and 2nd gel runs were done by isoelectric focusing and SDS-PAGE, respectively. 
Numerals at the bottom indicate pI values, and kDa values at right side indicate the molecular weights of 
the separated proteins. 

 

 

is capable of undergoing changes in the expression of 
various proteins in response to the materials. Therefore, 
in order to investigate the patterns of protein expression 
associated with a mugwort powder diet, 2-DE analysis 
was performed using 1.1 mg protein extracted from pig l. 
dorsi muscle, which is one of the most important meat 
cuts for human beings. After 2-DE separation of the 
proteins, quantitative Colloidal CBB staining revealed 
roughly 300 spots (Figure 1). The 2-DEs originating from 
the two different groups (C group, a basal diet and T 
group; a basal diet supplemented with 1.5% mugwort 
powder) were used to analyze the protein expression 
patterns associated with mugwort. A spot with different 
densities was selected through analysis of the gel images 
as a protein to show expression changes between groups. 
However, the spot selected as a protein showing an 
expression change was used only to show regular density 
changes of 2 to 3 spots among the four spots obtained 
per group.  

Although most spots were of similar density between 
the C and T groups, 12 spots showed different expres-
sion levels, and all the spots were of greater density in 
the T group (Figure 2). The spots with increased 
expression were described by mean intensity, as shown 
in Table 1. The density of spot 7002 dramatically 
increased by 4.66-fold, while spots 1004, 5001 and 8002 

 
 

 

increased more moderately by 2.51, 2.73 and 2.57 fold, 
respectively. The densities of spots 1106, 2001, 5002, 
5602 and 7102 were marginally increased by 1.35, 1.41, 
1.64, 1.69 and 1.60 fold, respectively. 
 

 

Properties of the proteins identified by PMF 

 

The spots with higher expression levels identified by PMF 
are shown in Table 2. Myosin light chain 2V and 
eukaryotic translation initiator factor 5A (elF-5A) were 
obtained with 61 and 58% sequence coverage, 
respectively. Myosin light polypeptide 3, F1-ATPase, 
peroxiredoxin-2, Kelch-related protein 1, MHC class 1 
antigen 7 (SLA-7), glycine amidinotransferase, and  
triosephosphate isomerase (Tpi 1; http://www. 
ncbi.nlm.nih.gov/protein /38512111) were obtained with 
sequence coverage below 44%. When compared with 
known proteins, the proteins discovered by PMF were 
highly likely to be correctly allocated because of their 
isoelectric point (pI value), their 2-DE position, and their 
molecular weight.  

Myosin is the most abundant contraction molecule in 
mammalian skeletal muscle, and it relates directly to the 
quality of pork meat. Although the heavy chain of myosin 
has been studied with respect to skeletal pork meat 



   
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 

 

Figure 2. Comparative analysis of protein expression patterns with and without dietary mugwort powder. (A) and (B) 
indicate protein patterns of pig longissimus dorsi muscle grown on diets with and without mugwort. The enhanced spots 
are marked by numerals. 

 

 

Table 1. Proteins from pig l. dorsi muscle exhibiting changes in expression due to dietary mugwort powder.  
 

 

SSP
1)

 MW
2)

 PI
3)

 

Mean intensity Mean intensity Fold variation: 
 

 of C
4)

 of T
5)

 T versus C 
 

 3 19.69 4.34 540 ± 235
6)

 1055 ± 519 1.95 
 

 1004 15.58 4.68 309 ± 116 774 ± 366 2.51 
 

 1106 27.06 4.64 3292 ± 733 4442 ± 1773 1.35 
 

 1405 55.91 4.58 569 ± 161 1020 ± 765 1.79 
 

 2001 24.12 4.69 817 ± 128 1153 ± 521 1.41 
 

 2601 78.37 4.69 295 ± 153 574 ± 450 1.95 
 

 5001 19.98 6.23 357 ± 331 973 ± 825 2.73 
 

 5002 24.42 6.48 309 ± 417 508 ± 256 1.64 
 

 5602 76.14 5.98 551 ± 256 933 ± 530 1.69 
 

 7002 15.67 7.69 316 ± 65 1472 ± 1475 4.66 
 

 7102 28.79 7.95 2930 ± 73 4692 ± 889 1.60 
 

 8002 15.53 8.10 2550 ± 44 6559 ± 2333 2.57 
  

1)
SSP; standard spot protein, 

2)
MW; molecular weight in kDa, 

3)
PI; isoelectric point, 

4)
Pig fed basal diet without mugwort, 

5)
Basal diet + 

mugwort powder 1.5%, 
6)

standard deviation. 
 

 

muscle by various methods (Bee et al., 1999; Gunawan 
et al., 2007; Lin and Hsu, 2005), studies involving other 
tissue types and myosin light chain have yet to be 
conducted. The protein elF-5A has been widely observed 
in all eukaryotic cells, and disruption of the gene 
encoding this protein causes the arrest of cell growth, cell 
death, and/or differentiation of cancer cells (Jao and Yu 
Chen, 2002). F1-ATPase mediates ATP production in 
mitochondria (Boyer, 1997). Although F1-ATPase chain D 
subunit d (Zhang et al., 2000), is one of the components 
of this complex, we do not know the reason why only this 

 
 

 

subunit shows increased expression. If F1-ATPase chain 
D acts to recruit the F1-ATPase complex or enhance its 
activity, it is a reasonable hypothesis that chain D would 
have an effect on meat quality. Muscle fiber is divided into 
types 1, 2a, and 2b. Type 1 maintains a high number of 
mitochondria, whereas type 2b has fewer of this organelle 
(Cieslak et al., 2000; Kim et al., 2009). Since F1-ATPase 
is one of the major components of mitochondria, an 
increase of F1-ATPase might lead to an increase of type 1 
fiber containing abundant mitochondria. Therefore, it was 
assumed that an increase in F1-ATPase 



  
 
 

 
Table 2. Proteins identified by PMF.  

 

Spot Predicted protein 
Accession number Sequence pI/MW 

 

(source) coverage (%) (kDa)  

  
 

3 myosin light chain 2V NP_998956 61 4.8/18.87 
 

1004 eukaryotic translation initiation factor 5A NP_001003658 58 5.1/17.04 
 

 similar to Myosin light polypeptide 3 (Myosin light chain 1, slow-twitch    
 

1106 muscle B/ventricular isoform) (MLC1SB) (Ventricular/slow twitch myosin XP_533849 43 5.0/22.52 
 

 alkali light chain) (Cardiac myosin light chain-1) (CMLC1) isoform 1    
 

 Chain D, The Structure of Bovine F1-Atpase    
 

1405 Covalently Inhibited With 1NBM_D 38 5.0/51.46 
 

 4-Chloro-7-Nitrobenzofurazan    
  

 
2001 

 
 

2601 

 
5001 

 
5002 

 
Peroxiredoxin-2 (Thioredoxin peroxidase 1) (Thioredoxin-dependent 

peroxide reductase 1) (Thiol-specific antioxidant protein) (TSA) 
 
similar to Kelch repeat and BTB domain containing protein 10 

(Kelch-related protein 1) (Kel-like protein 23) (Sarcosin)  
isoform 2 

 
MHC class I antigen 7  
Glycine amidinotransferase  
(L-arginine:glycine amidinotransferase)  
(Transamidinase) (AT) 

  
 

P52552 34 4.7/13.82 

XP_535949 21 5.1/68.88 

NP_998933 21 9.0/46.05 

P50441 14 6.2/44.63 

 

7102   Tpi 1 protein AAH61781 44 7.1/ 27.21 
 

Pl, isoelectric point; MW, molecular weight. 
 

 

might induce a change in the quality of pig meat. Since 
peroxiredoxin-2 exists in mitochondria and plays a role in 
electron transport (Gromer et al., 2004), an increase in 
this protein could correlate with mitochondrial number, 
similarly to F1-ATPase.  

Kelch-related protein 1 has been reported to play a 
critical role in the maintenance of an ordered cyto-
skeleton (Jiang et al., 2005). MHC class I immune 
responses react against foreign pathogens and 
transplanted tissue. MHC class I molecules are divided 
into classical and non-classical types, and SLA-7 is 
included in the non-classical type (Joyce et al., 2008). 
Although this protein is induced as a result of immune 
responses due to physiological activating materials in 
mugwort, a definite function of the protein remains to be 
discovered. Since glycine amidinotransferase relates to 
the biosynthesis of creatine in the liver and pancreas 
(Engelke et al., 2009), we do not know the reason why 
this protein's expression is higher in this tissue. Tpi 
protein is an enzyme that mediates the reaction from 
dihydroxyacetone phosphate (DHAP) to glycerol-
aldehyde-3-phosphate, and it plays an essential role in 
the Embden-Meyerhof pathway (EMP). Since increases 
in this enzyme were assumed to correlate with 
mitochondrial numbers as mentioned previously, the 
increased amount of Tpi would lead to increased sugar 
utilization by promoting the complete oxidation of sugar. 
Therefore, the increased Tpi protein might be involved in 
energy utilization owing to the increased growth rate and 
maintenance energy requirements. 

 
 

 

Properties of proteins identified by CAF-MALDI 
sequencing 

 

The protein spots that could not be identified via PMF 
were analyzed by CAF-MALDI sequencing. As shown in 
Table 3, serum albumin precursor and two types of 
myoglobins were identified by CAF-MALDI sequencing. 
Generally, serum albumin, which has the signal peptide 
from serum albumin precursor consisting of 18 amino 
acids removed, plays an essential role in maintaining 
osmotic pressure for the approximate distribution of 
cellular fluidity in the extracellular matrix and between 
cells. Serum albumin also plays other roles as a serum 
carrier via nonspecific interactions with hydrophobic 
steroid hormones as well as a transport protein for hemin 
and fatty acids (Roche et al., 2008). Therefore, the 
increase of this precursor might be involved in promoting 
physiological activation in pigs due to mugwort. 
Myoglobin transfers oxygen to muscle cells. Since the 
mitochondrial numbers in pigs fed with mugwort were 
assumed to indirectly increase as described in the cases 
of F1-ATPase and peroxiredoxin-2, following the increase 
in the overall activation of oxidative electron transport, it 
was predicted that myoglobin in muscle helps to promote 
the supply of oxygen, which is the final electron acceptor. 
Two myoglobin spots might have been obtained as 
derivatives originating from the chemical treatment 
process.  

In summary, the effects of mugwort treatment poten-
tially include increases in growth, ordered arrangement of 



 
 
 

 
Table 3. Proteins identified by CAF-MALDI sequencing.  

 
 

Spot Identified protein 
Accession number Identified amino acid 

pI/MW (kDa)  

 
(source) sequence  

    
 

 5602 Serum albumin precursor P07724 DVFLGTFLYEYSR 5.98/76.14 
 

 7002 Myoglobin 1 1606205A HGBTVLTALGGILK 7.69/15.67 
 

 8002 Myoglobin 2 1606205A HGBTVLTALGGILK 8.10/15.53 
 

 

 

the cytoskeleton, immune responses, aerobic respiration, 
oxygen transport, and type 1 muscle fiber, which contains 
the highest amount of mitochondria. 

 

ACKNOWLEDGEMENTS 
 
This work was carried out with the support of the 
“Cooperative Research Program for Agriculture Science 
and Technology Development (Project No. PJ004186)” 
Rural Development Administration, Republic of Korea, 
Gyeongnam Swine Cluster Agency, and also was 
supported by Priority Research Centers Program through 
the National Research Foundation of Korea (NRF) funded 
by the Ministry of Education, Science and Technology 
(2009-0093813). 
 

 
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