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Fluorescent quantitation method for differentiating the nativity of green fluorescent protein

Chew FN, Tan WS, Tey BT

J Biosci Bioeng, 2011 Feb;111(2):246-8.
PMID: 21036662 DOI: 10.1016/j.jbiosc.2010.10.004

A gel imaging method was employed to quantitate the GFP that had been subjected to denaturation and degradation treatments. This method is able to differentiate the nativity of GFP by relating the observed changes in the position of fluorescent bands which is unable to be detected using the spectrofluorometric method.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Recovery of laccase from processed Hericium erinaceus (Bull.:Fr) Pers. fruiting bodies in aqueous two-phase system

Rajagopalu D, Show PL, Tan YS, Muniandy S, Sabaratnam V, Ling TC

J Biosci Bioeng, 2016 Sep;122(3):301-6.
PMID: 26922478 DOI: 10.1016/j.jbiosc.2016.01.016

The feasible use of aqueous two-phase systems (ATPSs) to establish a viable protocol for the recovery of laccase from processed Hericium erinaceus (Bull.:Fr.) Pers. fruiting bodies was evaluated. Cold-stored (4.00±1.00°C) H. erinaceus recorded the highest laccase activities of 2.02±0.04 U/mL among all the processed techniques. The evaluation was carried out in twenty-five ATPSs, which composed of polyethylene glycol (PEG) with various molecular weights and potassium phosphate salt solution to purify the protein from H. erinaceus. Optimum recovery condition was observed in the ATPS which contained 17% (w/w) PEG with a molecular weight of 8000 and 12.2% (w/w) potassium phosphate solution, at a volume ratio (VR) of 1.0. The use of ATPS resulted in one-single primary recovery stage process that produced an overall yield of 99% with a purification factor of 8.03±0.46. The molecular mass of laccases purified from the bottom phase was in the range of 55-66 kDa. The purity of the partitioned laccase was confirmed with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Cloning, expression and display of the PreS domain of hepatitis B virus on filamentous bacteriophage M13

Kok WL, Yusoff K, Nathan S, Tan WS

J. Biochem. Mol. Biol. Biophys., 2002 Feb;6(1):55-8.
PMID: 12186783

The PreS domain of hepatitis B virus (HBV) is believed to be involved in virion assembly and attachment to a hepatocyte receptor during infection. In order to study the functions of this region, we fused it to the g3p protein of bacteriophage M13 that allows the fusion protein to be displayed at the tip of the filament. The fusion protein was detected by the anti-E tag antibody on a Western blot. The polypeptide in a soluble form was produced by transfecting a non-suppressor E. coli host cell with the recombinant phagemid. The soluble protein was detected in cytoplasm, in the periplasmic space and also in the medium. The functional display of the PreS domain would provide an alternative means to study its interactions with the nuleocapsid and hepatocytes.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Emulsifying and foaming properties of ultraviolet-irradiated egg white protein and sodium caseinate

Kuan YH, Bhat R, Karim AA

J Agric Food Chem, 2011 Apr 27;59(8):4111-8.
PMID: 21401213 DOI: 10.1021/jf104050k

The physicochemical and functional properties of ultraviolet (UV)-treated egg white protein (EW) and sodium caseinate (SC) were investigated. UV irradiation of the proteins was carried out for 30, 60, 90, and 120 min. However, the SC samples were subjected to extended UV irradiation for 4 and 6 h as no difference was found on the initial UV exposure time. Formol titration, SDS-PAGE, and FTIR analyses indicated that UV irradiation could induce cross-linking on proteins and led to improved emulsifying and foaming properties (P < 0.05). These results indicated that the UV-irradiated EW and SC could be used as novel emulsifier and foaming agents in broad food systems for stabilizing and foaming purposes.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Proteomic analysis of antihypertensive proteins in edible mushrooms

Lau CC, Abdullah N, Shuib AS, Aminudin N

J Agric Food Chem, 2012 Dec 19;60(50):12341-8.
PMID: 23190208 DOI: 10.1021/jf3042159

Mushrooms are high in protein content, which makes them potentially a good source of antihypertensive peptides. Among the mushrooms tested, protein extracts from Pleurotus cystidiosus (E1Pc and E5Pc) and Agaricus bisporus (E1Ab and E3Ab) had high levels of antihypertensive activity. The protein extracts were fractionated by reverse-phase high-performance liquid chromatography (RPHPLC) into six fractions. Fraction 3 from E5Pc (E5PcF3) and fraction 6 from E3Ab (E3AbF6) had the highest antihypertensive activities. SDS-PAGE analysis showed E5PcF3 consisted mainly of low molecular weight proteins, whereas E3AbF6 contained a variety of high to low molecular weight proteins. There were 22 protein clusters detected by SELDI-TOF-MS analysis with five common peaks found in E5PcF3 and E3AbF6, which had m/z values in the range of 3940-11413. This study suggests that the antihypertensive activity in the two mushroom species could be due to proteins with molecular masses ranging from 3 to 10 kDa.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Latent polyphenol oxidases from sago log (Metroxylon sagu): partial purification, activation, and some properties

Onsa GH, bin Saari N, Selamat J, Bakar J

J Agric Food Chem, 2000 Oct;48(10):5041-5.
PMID: 11052775

Latent polyphenol oxidase (LPPO), an enzyme responsible for the browning reaction of sago starches during processing and storage, was investigated. The enzyme was effectively extracted and partially purified from the pith using combinations of nonionic detergents. With Triton X-114 and a temperature-induced phase partitioning method, the enzyme showed a recovery of 70% and purification of 4. 1-fold. Native PAGE analysis of the partially purified LPPO revealed three activity bands when stained with catechol and two bands with pyrogallol. The molecular masses of the enzymes were estimated by SDS-PAGE to be 37, 45, and 53 kDa. The enzyme showed optimum pH values of 4.5 with 4-methylcatechol as a substrate and 7.5 with pyrogallol. The LPPO was highly reactive toward diphenols and triphenols. The activity of the enzyme was greatly enhanced in the presence of trypsin, SDS, ethanol, and linoleic acid.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Fulltext Expression of recombinant E1 Glycoprotein of Chikungunya virus in Baculovirus expression system

Sum, Magdline Sia Henry, Andrew, Anna, Maling, Milda Aren

Journal of Biochemistry, Microbiology and Biotechnology, 2015;3(1):26-29.
MyJurnal

Chikungunya is an acute febrile illness caused by chikungunya virus (CHIKV). In this study, the envelope E1 gene of CHIKV was cloned and expressed in a baculovirus system. The recombinant E1 protein with N-term 6-His residues protein was successfully expressed and purified as confirmed by SDS-PAGE and western blot analysis. The seroreactivity of the recombinant protein was evaluated in immunoassay for anti-CHIKV IgM and IgG antibodies. The recombinant antigen showed 69% sensitivity and 100% specificity for anti-CHIKV IgG by dot blot assay. Detection of anti-CHIKV IgM by dot assay showed 79% sensitivity and 100% specificity. No cross reactivity of the antigen was observed with anti-dengue virus serum samples. The results strongly support that the recombinant E1 protein has potential to be used as diagnostic antigen. The used of the antigen in a dot blot assay gives an advantage for laboratory detection without the need of any specialised equipment.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Purification and comparison of intracellular proteinase A in Candida spp. isolates from Malaysian and Iranian patients and infected mice

Amri Saroukolaei S, Pei Pei C, Shokri H, Asadi F

J Mycol Med, 2012 Jun;22(2):149-59.
PMID: 23518017 DOI: 10.1016/j.mycmed.2012.01.002

To compare the specific intracellular proteinase A activity in clinical isolates of Candida species isolated from Iranian and Malaysian patients, the blood and kidneys of mice infected by Candida cells isolated from these human patients.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Identification of Common and Novel Major Crab Allergens in Scylla tranquebarica and the Allergen Stability in Untreated and Vinegar-treated Crab

Jasim HA, Misnan R, Yadzir ZHM, Abdullah N, Bakhtiar F, Arip M, et al.

Iran J Allergy Asthma Immunol, 2021 Feb 11;20(1):76-87.
PMID: 33639634 DOI: 10.18502/ijaai.v20i1.5414

Crab allergy is reported as a serious form of food allergy in many countries. This study was aimed to identify the major allergens of the local mud crab, Scylla tranquebarica (S. tranquebarica), and subsequently, determine the effect of vinegar treatments on the crab allergens. Crab muscles were treated with synthetic and natural vinegar. Crab proteins were then extracted from the untreated and vinegar-treated crabs. All extracts were then fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and analyzed by immunoblotting; using sera from crab-allergic patients. The crab proteins were then further fractionated by two-dimensional electrophoresis (2-DE)and analyzed by mass spectrometry (MS). The untreated crab had 38 protein bands, while that was only a few bands between 18 to 73 kDa for the vinegar-treated crabs. Immunoblotting of untreated crab revealed 20 IgE-binding bands, whereas the vinegar-treated crabs could only retain a few IgE-binding bands. Five major allergens were identified with molecular weightsof38, 42, 49, 63, and 73 kDa in the untreated crab. In contrast, the vinegar-treated crabs had only a few major allergens with molecular weights of 38, 42, and 73 kDa. MS identified the 43 and 49 kDa as arginine kinase, while the 38, 63, and 73 kDa were identified as tropomyosin, actin, and hemocyanin, respectively. Inconclusion, we found three common major allergens for S. tranquebarica including tropomyosin, arginine kinase, and actin, and one novel allergen known as hemocyanin. All the major allergens could retain minimal allergenic capability in vinegar-treated crabs, suggesting that vinegar treatments might be useful to reduce crab allergenicity. These data would assist the clinicians in the management of crab-allergic patients worldwide.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Complete Genome Sequence of Proteus mirabilis Phage pPM_01 Isolated from Raw Sewage

Wirjon IA, Lau NS, Arip YM

Intervirology, 2016;59(5-6):243-253.
PMID: 28384626 DOI: 10.1159/000468987

OBJECTIVES: Phage pPM_01 was previously isolated from a raw sewage treatment facility located in Batu Maung, Penang, Malaysia, and it was highly lytic against Proteus mirabilis, which causes urinary tract infections in humans. In this paper, we characterize the biology and complete genome sequence of the phage.
METHODS AND RESULTS: Transmission electron microscopy revealed phage pPM_01 to be a siphovirus (the first reported virus to infect P. mirabilis), with its complete genome sequence successfully determined. The genome was sequenced using Illumina technology and the reads obtained were assembled using CLC Genomic Workbench v.7.0.3. The whole genome contains a total of 58,546 bp of linear double-stranded DNA with a G+C content of 46.9%. Seventy putative genes were identified and annotated using various bioinformatics tools including RAST, Geneious v.R7, National Center for Biotechnology Information (NCBI) BLAST, and tRNAscan-SE-v1.3 Search. Functional clusters of related potential genes were defined (structural, lytic, packaging, replication, modification, and modulatory). The whole genome sequence showed a low similarity to known phages (i.e., Enterobacter phage Enc34 and Enterobacteria phage Chi). Host range determination and SDS-PAGE analysis were also performed.
CONCLUSIONS: The inability to lysogenize a host, the absence of endotoxin genes in the annotated genome, and the lytic behavior suggest phage pPM_01 as a possible safe biological candidate to control P. mirabilis infection.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Leuconostoc durionis sp. nov., a heterofermenter with no detectable gas production from glucose

Leisner JJ, Vancanneyt M, Van der Meulen R, Lefebvre K, Engelbeen K, Hoste B, et al.

Int J Syst Evol Microbiol, 2005 May;55(Pt 3):1267-1270.
PMID: 15879266 DOI: 10.1099/ijs.0.63434-0

Three lactic acid bacterial (LAB) strains obtained from a Malaysian acid-fermented condiment, tempoyak (made from pulp of the durian fruit), showed analogous but distinct patterns after screening by SDS-PAGE of whole-cell proteins and comparison with profiles of all recognized LAB species. 16S rRNA gene sequencing of one representative strain showed that the taxon belongs phylogenetically to the genus Leuconostoc, with its nearest neighbour being Leuconostoc fructosum (98 % sequence similarity). Biochemical characteristics and DNA-DNA hybridization experiments demonstrated that the strains differ from Leuconostoc fructosum and represent a single, novel Leuconostoc species for which the name Leuconostoc durionis sp. nov. is proposed. The type strain is LMG 22556(T) (= LAB 1679(T) = D-24(T) = CCUG 49949(T)).

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Fulltext Self-assembled insulin and nanogels polyelectrolyte complex (Ins/NGs-PEC) for oral insulin delivery: characterization, lyophilization and in-vivo evaluation

Mudassir J, Darwis Y, Muhamad S, Khan AA

Int J Nanomedicine, 2019;14:4895-4909.
PMID: 31456636 DOI: 10.2147/IJN.S199507

Introduction: Insulin is given by injection, because when administered orally, it would be destroyed by enzymes in the digestive system, hence only about 0.1% reaches blood circulation. The purpose of the present study was to use pH sensitive polyelectrolyte methyl methacrylate (MMA)/itaconic acid (IA) nanogels as carriers in an attempt to improve absorption of insulin administered orally. Methods: Insulin (Ins) was incorporated into the MMA/IA nanogels (NGs) using the polyelectrolyte complexation (PEC) method to form Ins/NGs-PEC. Several parameters, including Ins:NGs ratio, pH, incubation time and stirring rate were optimized during preparation of InsNGs-PEC. The prepared formulations were characterized in terms of particle size (PS), polydispersity index (PdI), zeta potential (ZP) and percent entrapment efficiency (% EE). Results: The optimized InF12 nanogels had a PS, PdI, ZP and %EE of 190.43 nm, 0.186, -16.70 mV and 85.20%, respectively. The InF12 nanogels were lyophilized in the presence of different concentrations of trehalose as cryoprotectant. The lyophilized InF12 containing 2%w/v trahalose (InF12-Tre2 nanogels) was chosen as final formulation which had a PS, PdI, ZP and %EE of 430.50 nm, 0.588, -16.50 mv and 82.10, respectively. The in vitro release of insulin from InF12-Tre2 nanogels in the SGF and SIF were 28.71% and 96.53%, respectively. The stability study conducted at 5±3°C for 3 months showed that lnF12-Tre2 nanogels were stable. The SDS-PAGE assay indicated that the primary structure of insulin in the lnF12-Tre2 nanogels was intact. The in-vivo study in the diabetic rats following oral administration of InF12-Tre2 nanogels at a dose of 100 IU/kg body weight reduced blood glucose level significantly to 51.10% after 6 hours compared to the control groups. Conclusions: The pH sensitive MMA/IA nanogels are potential carriers for oral delivery of insulin as they enhanced the absorption of the drug.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Fulltext Role of α-helical structure in organic solvent-activated homodimer of elastase strain K

Rahman RN, Salleh AB, Basri M, Wong CF

Int J Mol Sci, 2011;12(9):5797-814.
PMID: 22016627 DOI: 10.3390/ijms12095797

Recombinant elastase strain K overexpressed from E. coli KRX/pCon2(3) was purified to homogeneity by a combination of hydrophobic interaction chromatography and ion exchange chromatography, with a final yield of 48% and a 25-fold increase in specific activity. The purified protein had exhibited a first ever reported homodimer size of 65 kDa by SDS-PAGE and MALDI-TOF, a size which is totally distinct from that of typically reported 33 kDa monomer from P. aeruginosa. The organic solvent stability experiment had demonstrated a stability pattern which completely opposed the rules laid out in previous reports in which activity stability and enhancement were observed in hydrophilic organic solvents such as DMSO, methanol, ethanol and 1-propanol. The high stability and enhancement of the enzyme in hydrophilic solvents were explained from the view of alteration in secondary structures. Elastinolytic activation and stability were observed in 25 and 50% of methanol, respectively, despite slight reduction in α-helical structure caused upon the addition of the solvent. Further characterization experiments had postulated great stability and enhancement of elastase strain K in broad range of temperatures, pHs, metal ions, surfactants, denaturing agents and substrate specificity, indicating its potential application in detergent formulation.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Fulltext Recombinant human adiponectin as a potential protein for treating diabetic tendinopathy promotes tenocyte progenitor cells proliferation and tenogenic differentiation in vitro

Rothan HA, Suhaeb AM, Kamarul T

Int J Med Sci, 2013;10(13):1899-906.
PMID: 24324367 DOI: 10.7150/ijms.6774

Adiponectin is an adipocyte-secreting hormone that increases cell sensitivity to insulin. It has been previously demonstrated that this hormone protects against Type II Diabetes and, is found to concurrently promote cell proliferation and differentiation. It is postulated that diabetic patients who suffer from tendinopathy may benefit from using adiponectin, which not only improves the metabolism of diabetic ridden tenocytes but also promotes progenitor cell proliferation and differentiation in tendons. These changes may result in tendon regeneration, which, in diabetic tendinopathy, is difficult to treat. Considering that such findings have yet to be demonstrated, a study was thus conducted using diabetic ridden human tenocyte progenitor cells (TPC) exposed to recombinant adiponectin in vitro. TPC were isolated from tendons of diabetic patients and exposed to 10 μg/ml adiponectin. Cell proliferation rate was investigated at various time points whilst qPCR were used to determine the tenogenic differentiation potential. The results showed that adiponectin significantly reduced blood glucose in animal models. The proliferation rate of adiponectin-treated TPCs was significantly higher at 6, 8 and 10 days as compared to untreated cells (p<0.05). The levels of tenogenic genes expression (collagen I, III, tenomodulin and scleraxis) were also significantly upregulated; whilst the osteogenic (Runx2), chondrogenic (Sox9) and adipogenic (PPARУγ) gene expressions remained unaltered. The results of this study suggest that adiponectin is a potential promoter that not only improves diabetic conditions, but also increases tendon progenitor cell proliferation and differentiation. These features supports the notion that adiponectin may be potentially beneficial in treating diabetic tendinopathy.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Identification of lactic acid bacteria constituting the predominating microflora in an acid-fermented condiment (tempoyak) popular in Malaysia

Leisner JJ, Vancanneyt M, Rusul G, Pot B, Lefebvre K, Fresi A, et al.

Int J Food Microbiol, 2001 Jan 22;63(1-2):149-57.
PMID: 11205946

Tempoyak is a traditional Malaysian fermented condiment made from the pulp of the durian fruit (Durio zibethinus). Salt is sometime added to proceed fermentation at ambient temperature. In various samples obtained from night markets, lactic acid bacteria (LAB) were the predominant microorganisms, ranging from log 8.4 to log 9.2 cfu g(-1). No other microorganisms were present to such a level. These samples contained reduced amount of saccharose, glucose and fructose but increased amount of D- and L-lactic acid and acetic acid compared with samples of non-fermented durian fruit. Sixty-four isolates of LAB were divided into five groups by use of a few phenotypic tests. A total of 38 strains of LAB were selected for comparison by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of their whole cell protein patterns with a SDS-PAGE database of LAB. These strains were also examined for their carbohydrate fermentation patterns by use of API 50 CH. Isolates belonging to the Lactobacillus plantarum group were shown to be the predominant members of the LAB flora. In addition, isolates belonging to the Lactobacillus brevis group, Leuconostoc mesenteroides, Lactobacillus mali, Lactobacilus fermentum and an unidentified Lactobacillus sp. were also observed. A high degree of diversity among isolates belonging to the Lb. plantarum group was demonstrated by analysis of their plasmid profiles.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
SDS-PAGE electrophoretic property of human chorionic gonadotropin (hCG) and its beta-subunit

Gam LH, Latiff A

Int J Biol Sci, 2005;1(3):103-9.
PMID: 16094462

The microheterogeneity property of hCG with regards to its sialic acid contents resulted in variable mobility of the glycoprotein in SDS-PAGE. The intact hCG molecule is composed of two dissimilar subunits, namely alpha- and beta-subunits. The identification of hCG bands in SDS-PAGE was accomplished by the immunoblotting experiment, whereby the antibody directed toward the specific region of beta-subunit of hCG was used. The data shows that the different mobility of intact hCG was attributed to the different degree of desialylation of the glycoprotein. Nevertheless, unlike the intact hCG, the mobility of its beta-subunit was not affected by its variety sialic acid content. This characteristic of beta-hCG is beneficial when semi-quantification of total hCG is required. Quantification of hCG using the HPLC-reversed phase C18 analytical column is not possible as the glycoprotein was eluted in multiple fractions at different retention times. The identification of denatured hCG (HPLC eluted fractions) was carried out by immunoblotting experiment whilst immunoassay technique failed to detect its presence in any fraction.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel/methods*
Enzymatic hydrolysis: Sialylated mucin (SiaMuc) glycoprotein of edible swiftlet's nest (ESN) and its molecular weight distribution as bioactive ESN SiaMuc-glycopeptide hydrolysate

Hui Yan T, Lim SJ, Babji AS, Rawi MH, Sarbini SR

Int J Biol Macromol, 2021 Apr 01;175:422-431.
PMID: 33561458 DOI: 10.1016/j.ijbiomac.2021.02.007

Bioactive edible swiftlet's nest (ESN) sialylated-mucin (SiaMuc) hydrolysate is produced by alcalase hydrolysis. Enzymatic hydrolysis of ESN breakdown high-valued ESN SiaMuc-glycoprotein into bioactive SiaMuc-glycopeptide. This is a breakthrough for the issue of insolubility and low extraction rate in ESN, and even increases the bioavailability of ESN nutritional functionality and health benefits. Hydrolysis of ESN SiaMuc-glycoprotein was performed for 1 to 4 h and its effect on physicochemical properties, molecular weight (MW) distribution, SiaMuc-glycoprotein and glycopeptide integrity were determined. Other than improvement in solubility and bioavailability as SiaMuc-glycopeptide, results from SDS-PAGE revealed that MW of SiaMuc-glycoprotein decreased from 42.0-148.8 kDa to 17.7-142.7 kDa with increasing hydrolysis period. Further hydrolysis from maximized DH (90 min) showed an insignificant effect on the MW of ESN SiaMuc-glycopeptide and remained constant at 15.2 kDa. This highlights that enzymatic hydrolysis only influences macro SiaMuc-glycoprotein fractions (142.7, 115.3 and 102.7 kDa), while the majority of SiaMuc-glycopeptide fractions from 36.6-98.6 kDa remained intact. Conclusively, alcalase hydrolysis of ESN showed high recovery in the form of bioactive ESN SiaMuc-glycopeptide. Therefore, enzymatic biotechnology is an economic alternative applicable on ESN that broaden industrial utilization by reducing the MW without destroying the quality of bioactive SiaMuc-glycoprotein.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Intraspecific variation of isoenzymes in Taenia taeniaeformis

Okamoto M, Ito A, Kurosawa T, Oku Y, Kamiya M, Agatsuma T

Int J Parasitol, 1995 Feb;25(2):221-8.
PMID: 7622329

The technique of isoenzyme electrophoresis was applied to Japanese wild populations of Taenia taeniaeformis (isolated from Norway rats) and three laboratory reared isolates (KRN isolated from a Malaysian Norway rat, BMM from a Belgian house mouse and ACR from a Japanese gray red-backed vole). The average heterozygosities of Japanese wild populations were fairly small and total genetic variability was 0.0499. The genetic make-up of T. taeniaeformis in Norway rats was rather uniform in the whole of Japan. In KRN isolate, each of all 10 loci examined possessed the allele which was predominant in Japanese wild populations. Similarly, each of 9 loci in BMM isolate possessed the same alleles, but one of 2 alleles at HK locus was different from that in the others. T. taeniaeformis parasitizing house mice and rats were considered to be genetically closely related to each other. In ACR isolate, 7 out of 10 loci possessed different alleles from those in the other populations. It was considered that ACR isolate was genetically distant and its phylogenetic origin in Japan should be different from worms parasitizing Norway rats.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Fulltext Detection of glycoproteins from human erythrocytes of different ABO blood groups infected with Plasmodium falciparum

Chin, Ramon Beng Ong, Kim, Patricia Chooi Lim, Joon, Wah Mak

International e-Journal of Science, Medicine & Education, 2011;5(2):18-28.
MyJurnal

Background: Many proteins released by cells to the blood and other fluids are glycoproteins. One set of glycoproteins carry the ABO blood group determinants and glycoproteins have been shown to be vital in determining the structure and organization of plasma membranes. There is evidence suggesting their important role in cell-to-cell contact, adhesion, hormone interaction and vital transformation. Differences in proteins and glycoproteins in the different human blood groups may influence the invasion process of Plasmodium falciparum. The objectives of the study were to determine whether there are any changes in proteins and glycoproteins of red blood cells upon infection by P. falciparum and whether these protein and glycoprotein changes differ in the various ABO blood groups.

Methods: A Malaysian strain of P. falciparum was cultured in vitro in red blood cells from A, B, O and AB blood groups. Protein and glycoprotein profiles of uninfected and P. falciparum- infected red blood cells from the different human ABO blood groups were analyzed by SDS-PAGE. For protein bands, the gels were stained with Coomassie blue while glycoproteins were visualized following staining of gels using GelCode ® Glycoprotein Staining Kit.

Results: Cell membranes of P. falciparum infected erythrocytes from different ABO blood groups have different glycoprotein profiles compared to uninfected cells. All the infected samples showed a prominent protein band of molecular weight 99 kDa which was not present in any of the uninfected samples while a 48 kDa band was seen in four out of the seven infected samples. The erythrocyte cell membranes of A and AB blood groups showed different glycoprotein profiles upon infection with P. falciparum when compared to those from blood groups B and O.

Conclusion: The two glycoproteins of molecular weights 99 kDa and 48 kDa should be further studied to determine their roles in the pathogenesis of malaria and as potential targets for drug and vaccine development.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel
Fulltext Identification of parvalbumin and two new thermolabile major allergens of Thunnus tonggol using a proteomics approach

Rosmilah M, Shahnaz M, Meinir J, Masita A, Noormalin A, Jamaluddin M

Int Arch Allergy Immunol, 2013;162(4):299-309.
PMID: 24193115 DOI: 10.1159/000354544

The longtail tuna (Thunnus tonggol) is widely consumed in Asia. Parvalbumin, the main major allergen of fish, has been well identified in multiple fish species, yet little is known about the allergenic proteins in T. tonggol. Thus, the aim of this study was to characterize the major allergens of T. tonggol using a proteomics approach.

Matched MeSH terms: Electrophoresis, Polyacrylamide Gel

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