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Analytical Biochemistry
Journal Prestige (SJR): 0.633
Citation Impact (citeScore): 2
Number of Followers: 225  
  Hybrid Journal Hybrid journal (It can contain Open Access articles)
ISSN (Print) 0003-2697 - ISSN (Online) 1096-0309
Published by Elsevier Homepage  [3204 journals]
  • How versatile is the use of ultrafiltration to study biointeractions of
           therapeutic metallodrugs'
    • Abstract: Publication date: Available online 26 March 2020Source: Analytical BiochemistryAuthor(s): Lidia S. Foteeva, Olga V. Kuznetsova, Bernhard K. Keppler
  • Possible Artefacts of Antioxidant Assays Performed in the Presence of
           Nitroxides and Nitroxide-containing Nanoparticles
    • Abstract: Publication date: Available online 25 March 2020Source: Analytical BiochemistryAuthor(s): Monika Pichla, Grzegorz Bartosz, Natalia Pieńkowska, Izabela Sadowska-Bartosz
  • Identifying transglutaminase reaction products via mass spectrometry as
           exemplified by the MUC2 mucin - Pitfalls and traps
    • Abstract: Publication date: Available online 25 March 2020Source: Analytical BiochemistryAuthor(s): Liisa Arike, Gunnar C. Hansson, Christian V. Recktenwald
  • FTIR-based L-Asparaginase activity assay enables continuous measurements
           in optically dense media including blood plasma
    • Abstract: Publication date: Available online 23 March 2020Source: Analytical BiochemistryAuthor(s): Elena V. Kudryashova, Marina V. Pokrovskaya, Svetlana S. Alexandrova, Alexander A. Vinogradov, Nikolay N. Sokolov
  • Reliability factor for identification of amylolytic enzyme activity in the
           optimized starch-iodine assay
    • Abstract: Publication date: Available online 19 March 2020Source: Analytical BiochemistryAuthor(s): Aline L.O. Gaenssle, Marc J.E.C. van der Maarel, Edita Jurak
  • Very long-term stability of lipid biomarkers in human serum
    • Abstract: Publication date: Available online 19 March 2020Source: Analytical BiochemistryAuthor(s): Vladimira Muzakova, Piet K. Beekhof, Eugène H.J.M. Jansen
  • Study of imidazole performance as pseudo-affinity ligand in the
           purification of IgG from bovine milk
    • Abstract: Publication date: Available online 19 March 2020Source: Analytical BiochemistryAuthor(s): Pariya Pourrostam-Ravadaneg, Kazem D. Safa, Hassan Abbasi
  • Fluorescence-based biochemical analysis of human hepatitis B virus reverse
           transcriptase activity
    • Abstract: Publication date: 15 May 2020Source: Analytical Biochemistry, Volume 597Author(s): Tetsuya Toyoda, Yongxiang Wang, Yumei Wen, Yasuhito Tanaka
  • Development of a LAMP method for detecting the N75S mutant in
           SDHI-resistant Corynespora cassiicola
    • Abstract: Publication date: 15 May 2020Source: Analytical Biochemistry, Volume 597Author(s): Jiamei Zhu, Lingyan Zhang, Hong Li, Yangyang Gao, Wei Mu, Feng Liu
  • A Low-cost Paper-based Aptasensor for Simultaneous Trace-level Monitoring
           of Mercury (II) and Silver (I) ions
    • Abstract: Publication date: Available online 19 March 2020Source: Analytical BiochemistryAuthor(s): Zahra Khoshbin, Mohammad Reza Housaindokht, Asma Verdian
  • Introduction of a New Method for Two-Dimensional NMR Quantitative Analysis
           in Metabolomics Studies
    • Abstract: Publication date: Available online 18 March 2020Source: Analytical BiochemistryAuthor(s): Lin Jiang, Kevin Howlett, Kristen Patterson, Bo Wang
  • Simultaneous monitoring of the bioconversion from lysine to glutaric
           acidby ethyl chloroformate derivatization and gas chromatography-mass
    • Abstract: Publication date: Available online 16 March 2020Source: Analytical BiochemistryAuthor(s): Yeong-Hoon Han, Tae-Rim Choi, Ye-Lim Park, Hun-Suk Song, Yong-Keun Choi, Hyun-Joong Kim, Shashi Kant Bhatia, Ranjit Gurav, Kyungmoon Park, See-Hyoung Park, Wooseong Kim, Yung-Hun Yang
  • Biomolecular condensates in cell biology and virology: phase-separated
           membraneless organelles (MLOs)
    • Abstract: Publication date: Available online 16 March 2020Source: Analytical BiochemistryAuthor(s): Pravin B. Sehgal, Jenna Westley, Kenneth M. Lerea, Susan DiSenso-Browne, Joseph D. Etlinger
  • Re-evaluation of the 18 non-human protein standards used to create the
           Empirical Statistical Model for Decoy Library Searching
    • Abstract: Publication date: Available online 16 March 2020Source: Analytical BiochemistryAuthor(s): Thanusi Thavarajah, Monika Tucholska, Pei-Hong Zhu, Peter Bowden, John G. Marshall
  • Improving the stability of the malachite green method for the
           determination of phosphate using Pluronic F68
    • Abstract: Publication date: Available online 9 March 2020Source: Analytical BiochemistryAuthor(s): Santiago A. Martínez Gache, Alvaro A. Recoulat Angelini, M. Lurdes Sabeckis, F. Luis González Flecha
  • Establishment of a 1, 4, 7, 10-tetraazacyclododecane-1,4,7,10-tetraacetic
           acid mono-N-hydroxysuccinimide ester (DOTA-NHS-ester) based lectin
           microarray for efficiently detecting serum glycans in gastric cancers
    • Abstract: Publication date: Available online 7 March 2020Source: Analytical BiochemistryAuthor(s): Yi Gao, Song-Guo Li, Qian Liu, Sheng-Sheng Liu, Lei Ye, Zi-Jian Song, Wei-Dong Du
  • Comparative metabolism of schaftoside in healthy and calcium oxalate
           kidney stone rats by UHPLC-Q-TOF-MS/MS method
    • Abstract: Publication date: Available online 4 March 2020Source: Analytical BiochemistryAuthor(s): Ruina Liu, Caifeng Meng, Zijian Zhang, Hongyun Ma, Tao Lv, Shuang Xie, Yimeng Liu, Chunying Wang
  • Metabolomic studies of amino acid analysis in Saccharomyces cells exposed
           to selenium and gamma irradiation
    • Abstract: Publication date: Available online 3 March 2020Source: Analytical BiochemistryAuthor(s): Josimar M. Batista, Maria J. Neves, Alline G. Pereira, Letícia S. Gonçalves, Helvécio C. Menezes, Zenilda L. Cardeal
  • Imaging of the ex vivo transglutaminase activity in liver macrophages of
           sepsis mice
    • Abstract: Publication date: Available online 3 March 2020Source: Analytical BiochemistryAuthor(s): Ting Su, Xian-Yang Qin, Yutaka Furutani, Wenkui Yu, Soichi Kojima
  • Cross-priming isothermal amplification combined with nucleic acid test
           strips for detection of meat species
    • Abstract: Publication date: Available online 2 March 2020Source: Analytical BiochemistryAuthor(s): Fangyuan Zheng, Sufang Li, Sunan Wang, Tao Feng, Zejun Jiang, Jiarong Pan
  • Analysis of testosterone-hydroxylated metabolites in human urine by Ultra
           High Performance Liquid Chromatography-Mass Spectrometry
    • Abstract: Publication date: Available online 29 February 2020Source: Analytical BiochemistryAuthor(s): Derly Constanza Escobar-Wilches, Arianna Ventura-Bahena, Ma. de Lourdes López-González, Luisa Torres-Sánchez, Mario Figueroa, Adolfo Sierra-Santoyo
  • Quick and convenient construction of lambda-cyhalothrin antigen for the
           generation of specific antibody
    • Abstract: Publication date: Available online 29 February 2020Source: Analytical BiochemistryAuthor(s): Nan Cui, Limin Cao, Jianxin Sui, Hong Lin, Xiangning Han, Xiangfeng Chen, Hanyi Xie, Xun Sun
  • Fast room temperature cloud point extraction procedure for
           spectrophotometric determination of phosphate in water samples
    • Abstract: Publication date: Available online 29 February 2020Source: Analytical BiochemistryAuthor(s): Denys Snigur, Alexander Chebotarev, Kseniia Bulat, Vitaliy Duboviy
  • Glycopeptide variable window SWATH for improved Data Independent
           Acquisition glycoprotein analysis
    • Abstract: Publication date: Available online 28 February 2020Source: Analytical BiochemistryAuthor(s): Chun Zhou, Benjamin L. Schulz
  • Quantitative structure–chromatographic retention relationship of
           synthesized peptides (HGRFG, NPNPT) and their derivatives
    • Abstract: Publication date: Available online 27 February 2020Source: Analytical BiochemistryAuthor(s): Xiangrong Yang, Huan Peng, Ningjuan Han, Zhongqi Zhang, Xiao Bai, Te Zhao, Jinli Zhao, Jianli Liu
  • Reporter cell assay-based functional quantification of TNF-α-antagonists
           in serum -- a proof-of-principle study for adalimumab
    • Abstract: Publication date: Available online 26 February 2020Source: Analytical BiochemistryAuthor(s): Lukas Schuster, Max Sauter, Philipp Uhl, Andreas Meid, Walter E. Haefeli, Johanna Weiss, Dirk Theile
  • Screening and Quantification of TNF-α Ligand from Angelicae Pubescentis
           Radix by Biosensor and UPLC-MS/MS
    • Abstract: Publication date: Available online 25 February 2020Source: Analytical BiochemistryAuthor(s): Liu Yang, Ajiao Hou, Song Wang, Jiaxu Zhang, Wenjing Man, Xinyue Guo, Bingyou Yang, Qiuhong Wang, Hai Jiang, Haixue Kuang
  • Some Novel Rare Earth Metal Ions complexes: Synthesis, Characterization,
           Luminescence and Biocidal Efficiency
    • Abstract: Publication date: Available online 24 February 2020Source: Analytical BiochemistryAuthor(s): Ayman A. Abdel Aziz, Mostafa A. Sayed
  • Flavonoids Interference in Common Protein Assays: Effect of Position and
           Degree of Hydroxyl Substitution
    • Abstract: Publication date: Available online 24 February 2020Source: Analytical BiochemistryAuthor(s): Rashim Singh, Rong Lu, Ming Hu
  • Innovation in the food industry using microbial transglutaminase: Keys to
           success and future prospects
    • Abstract: Publication date: Available online 22 February 2020Source: Analytical BiochemistryAuthor(s): Noriko MiwaTransglutaminase (TG) catalyzes cross-linking between the γ-carboxyamide groups of glutamine residues and the ε-amino groups of lysine residues in polypeptide chains, yielding ε- (γ-glutamyl) lysine (G-L) bonds. By forming a network structure in the protein via G-L bonds, it is possible to increase the viscosity of protein solutions or to cause gelation. Nearly thirty years have passed since microbial TG (MTG) appeared in the food enzyme market. Since the start of research and development, MTG has been used in fishery products such as kamaboko (boiled fish paste), meat products such as sausages, milk products such as yogurt, processed-soybean products such as tofu, and wheat products such as bread and noodles. MTG has provided effects such as adding new functions and reducing waste in food applications. The purpose of this review is to describe not only the history of research and development of TG but also the key aspects that have facilitated the great success of this process as a technology for enzymatically modifying protein-containing foods.Graphical abstractImage 1
  • Determination of homocysteine thiolactone in human urine by capillary zone
           electrophoresis and single drop microextraction
    • Abstract: Publication date: Available online 21 February 2020Source: Analytical BiochemistryAuthor(s): Krystian Purgat, Patrycja Olejarz, Izabella Kośka, Rafał Głowacki, Paweł KubalczykA simple, fast, sensitive and reproducible capillary zone electrophoresis (CZE) method with single drop microextraction (SDME) for determination of homocysteine thiolactone (HTL) in human urine has been developed and validated. The method is characterized by good precision, high accuracy, short analysis time and low consumption of reagents. The procedure consists only of few steps: urine sample centrifugation, dilution with phosphate buffer and methanol, chloroform addition onto the top of donor phase, on-line SDME in CE system, sample separation by CZE and ultraviolet detection of HTL at 240 nm. The background electrolyte was 0.1 M pH 4.75 phosphate buffer. Effective separation was achieved within 6.04 min under the separation voltage of 24 kV (∼110 μA). The LOQ and LOD for HTL were 50 and 25 nM urine, respectively. The calibration curve in urine showed linearity in the range of 50–200 nM, with R2 0.9995. The intra- and inter-day precision and recovery were 4.0–14.5% (average 8.7% and 9.3%) and 92.7–115.5% (average 103.6% and 104.8%), respectively. The procedure was successfully applied to analysis of urine samples.Graphical abstractImage 1
  • Glycoproteomic measurement of site-specific polysialylation
    • Abstract: Publication date: Available online 20 February 2020Source: Analytical BiochemistryAuthor(s): Ruby Pelingon, Cassandra L. Pegg, Lucia F. Zacchi, Toan K. Phung, Christopher B. Howard, Ping Xu, Matthew P. Hardy, Catherine M. Owczarek, Benjamin L. SchulzPolysialylation is the enzymatic addition of a highly negatively charged sialic acid polymer to the non-reducing termini of glycans. Polysialylation plays an important role in development, and is involved in neurological diseases, neural tissue regeneration, and cancer. Polysialic acid (PSA) is also a biodegradable and non-immunogenic conjugate to therapeutic drugs to improve their pharmacokinetics. PSA chains vary in length, composition, and linkages, while the specific sites of polysialylation are important determinants of protein function. However, PSA is difficult to analyse by mass spectrometry (MS) due to its high negative charge and size. Most analytical approaches for analysis of PSA measure its degree of polymerization and monosaccharide composition, but do not address the key questions of site specificity and occupancy. Here, we developed a high-throughput LC-ESI-MS/MS glycoproteomics method to measure site-specific polysialylation of glycoproteins. This method measures site-specific PSA modification by using mild acid hydrolysis to eliminate PSA and sialic acids while leaving the glycan backbone intact, together with protease digestion followed by LC-ESI-MS/MS glycopeptide detection. PSA-modified glycopeptides are not detectable by LC-ESI-MS/MS, but become detectable after desialylation, allowing measurement of site-specific PSA occupancy. This method is an efficient analytical workflow for the study of glycoprotein polysialylation in biological and therapeutic settings.Graphical abstractImage 1
  • Bona fide gene expression analysis of samples from the bovine reproductive
           system by microfluidic platform
    • Abstract: Publication date: Available online 20 February 2020Source: Analytical BiochemistryAuthor(s): Patricia Kubo Fontes, Anthony César de Souza Castilho, Eduardo Montanari Razza, Marcelo Fábio Gouveia NogueiraSample types such as those from reproductive systems often yield scarce material, which limits RT-qPCR analysis to only a few targets. Recently developed high-throughput systems can potentially change this scenario, however, the nanoliter scale of such platforms requires extra processing, e.g., preamplification, which needs to be defined through observation and experience. In order to establish best practices in high-throughput PCR approaches using samples from reproductive systems, we evaluated the Biomark™ HD performance using 11 different sample types from the bovine reproductive system: blastocyst (single/pool), oocyte (pool), cumulus, granulosa, and theca cells, oviduct tissue, fetal ovary, testicle (adult/fetal), and uterine horn. We observed that the preamplification step is not just reliable, but mandatory. Our results indicated that 14-preamplification cycles associated to 5- and 7-fold-dilution is the best approach for those samples. Additionally, the Biomark™ HD system has a high intra and inter reproducibility, therefore its performance in duplicate is unnecessary for the ΔCq analysis, taking in consideration the cutoff value 4 
  • Advances of aptamers screened by Cell-SELEX in selection procedure, cancer
           diagnostics and therapeutics
    • Abstract: Publication date: Available online 19 February 2020Source: Analytical BiochemistryAuthor(s): Yi Zhong, Jiayao Zhao, Fengling ChenAbstractAptamers are a class of short artificial single-stranded oligo(deoxy) nucleotides that can bind to different targets, which generated by Systematic Evolution of Ligands by Exponential Enrichment (SELEX). Due to excellent selectivity and high affinity to targets, aptamers hold considerable potential as molecular probe in diverse applications ranging from ensuring food safety, monitoring environment, disease diagnosis to therapy. This review highlights recent development and challenges about aptamers screened by Cell-SELEX, and its application about cancer diagnostics and therapeutics. Advances about some operation methods such as operation method and culture method in aptamers selection procedure were summarized in this paper. Some common challenges and technological difficulties such as nonspecific binding and biostability were discussed. Up to now, the recent endeavors about cancer diagnostic and therapeutic applications of aptamers are summarized and expatiated. Most of aptamers screened by Cell-SELEX took tumor cells as target cells, and such aptamers have been assembled to various aptasensor for cancer diagnosis. Aptamers conjugated various drugs or nanomaterials are functioned for cancer target therapy to improve drugs delivery efficiency and reduce side effects. Furthermore, the duplexed aptamer is discussed to be applied for cancer cells detection and some conflicts of theories about duplexed aptamer designs are analyzed.
  • Lateral flow assay using aptamer-based sensing for on-site detection of
           dopamine in urine
    • Abstract: Publication date: Available online 19 February 2020Source: Analytical BiochemistryAuthor(s): Shima Dalirirad, Andrew J. StecklA lateral flow assay using DNA aptamer-based sensing for the detection of dopamine in urine is reported. Dopamine duplex aptamers (hybridized sensor with capture probe) are conjugated to 40-nm Au nanoparticles (AuNPs) with 20T linkers. The detection method is based on the dissociation of the duplex aptamer in the presence of dopamine, with the sensor part undergoing conformational changes and being released from the capture part. Hybridization between the complementary DNA in the test line and the conjugated AuNP-capture DNA produces a red band, whose intensity is related to the dopamine concentration. The minimum detectable concentration obtained by ImageJ analysis was
  • Re-track: Software to analyze the retraction and protrusion velocities of
           neurites, filopodia and other structures
    • Abstract: Publication date: Available online 17 February 2020Source: Analytical BiochemistryAuthor(s): Sayed Iman Mousavi, Katherine M. Peace, Suzanne Scarlata, Erkan TüzelWe have developed new software, Re-track, that will quantify the rates of retraction and protrusion of structures emanating from the central core of a cell, such as neurites or filopodia. Re-Track, uses time-lapse images of cells in TIFF format and calculates the velocity of retraction or protrusion of a selected structure. The software uses a flexible moving boundary and has the ability to correct this boundary throughout analysis. Re-Track is fast, platform independent, and user friendly, and it can be used to follow biological events such as changes in neuronal connections, tip-growing cells such as moss, adaptive migration of cells, and similar behavior in non-biological systems.Graphical abstractImage 1
  • A sensitive LC-MS assay using derivatization with boron trifluoride to
           quantify curcuminoids in biological samples
    • Abstract: Publication date: Available online 17 February 2020Source: Analytical BiochemistryAuthor(s): Alexander J. Yoon, Haiqiang Wu, Roy D. Pan, Bruce Teter, Jack Cipolla, Edwin Chang, Luis Z. Avila, Saroj K. Basak, Eri Srivatsan, Marilene B. Wang, Greg M. Cole, Sally A. Frautschy, Phillip D. Hampton, Kym F. FaullA procedure is described to measure curcumin (C), demethoxycurcumin (DMC), bisdemethoxycurcumin (BDMC), tetrahydrocurcumim (TC) and their glucuronidated metabolites (CG, DMCG, and BDMCG) in plasma, brain, liver and tumor samples. The procedure involves converting the analytes to their boron difluoride derivatives and analyzing them by combined liquid chromatography coupled to an ion trap mass spectrometer operating in the negative ion MSn scan mode. The method has superb limits of detection of 0.01 nM for all curcuminoids and 0.5 nM for TC and the glucuroniated metabolites, and several representative chromatograms of biological samples containing these analytes are provided. In addition, the pharmacokinetic profile of these compounds in one human who daily consumed an over-the-counter curcuminoid product shows the peak and changes in circulating concentrations achieved by this mode of administration.Graphical abstractImage 1
  • Insights on the heparan sulphate-dependent externalisation of
           transglutaminase-2 (TG2) in glucose-stimulated proximal-like tubular
           epithelial cells
    • Abstract: Publication date: Available online 16 February 2020Source: Analytical BiochemistryAuthor(s): Giulia Furini, Izhar Burhan, Linghong Huang, Maria Pia Savoca, Adeola Atobatele, Tim Johnson, Elisabetta VerderioThe extracellular matrix crosslinking enzyme transglutaminase 2 (TG2) is highly implicated in tissue fibrosis that precedes end-stage kidney failure. TG2 is unconventionally secreted through extracellular vesicles in a way that depends on heparan sulphate (HS) proteoglycan syndecan-4 (Sdc4), the deletion of which reduces experimental kidney fibrosis as a result of lower extracellular TG2 in the tubule-interstitium. Here we establish a model of TG2 externalisation in NRK-52E tubular epithelial cells subjected to glucose stress. HS-binding TG2 mutants had reduced extracellular TG2 in transfected NRK-52E, suggesting that TG2-externalisation depends on an intact TG2 heparin binding site. Inhibition of N-ethylmaleimide sensitive factor (NSF) vesicle-fusing ATPase, which was identified in the recently elucidated TG2 kidney membrane-interactome, led to significantly lower TG2-externalisation, thus validating the involvement of membrane fusion in TG2 secretion. As cyclin-G-associated kinase (GAK) had emerged as a further TG2-partner in the fibrotic kidney, we investigated whether glucose-induced TG2-externalisation was accompanied by TG2 phosphorylation in consensus sequences of cyclin-dependent kinase (CDK). Glucose stress led to intense TG2 phosphorylation in serine/threonine CDK-target. TG2 phosphorylation by tyrosine kinases was also increased by glucose. Although the precise role of glucose-induced TG2 phosphorylation is unknown, these novel data suggest that phosphorylation may be involved in TG2 membrane-trafficking.Graphical abstractImage 1
  • Identification and characterization of substrates crosslinked by
           transglutaminases in liver and kidney fibrosis
    • Abstract: Publication date: Available online 13 February 2020Source: Analytical BiochemistryAuthor(s): Hideki Tatsukawa, Taishu Takeuchi, Yoshiki Shinoda, Kiyotaka HitomiAbstractThe transglutaminase (TGase) family consists of eight isozymes that catalyze the Ca2+-dependent crosslink formation between the glutamine and lysine residues of proteins. In the pathogenesis of various chronic diseases, among the TGase isozymes, TG2 in particular was upregulated and contributed to a critical role in fibrosis development and progression via the stabilization of extracellular matrix proteins and activation of TGF-β. Although TG2 has been considered a key enzyme in fibrosis, the causative role of TG2 and involvement of other isozymes remain unclear. We have recently developed a comprehensive analysis method targeting the isozyme-specific substrates of TGase in liver and kidney fibrosis. In this review article, we introduced the previously developed method for determining the activity and tissue distribution of TGase and for the detecting and identifying TGase substrates in an isozyme-specific manner. Using our comprehensive analysis method, we newly characterized the overlapped profile data regarding potential substrates of TG1 and TG2 that have been identified in liver and kidney fibrosis to date. Our results obtained by comparing the specificity and similarity of potential TGase substrates between different tissue fibrosis models provide a deeper understanding regarding the specific and common pathways in disease pathogenesis and progression.
  • A dicyanoisophorone-based, near-infrared, lysosome-targeting pH sensor
           with an extremely large Stokes shift
    • Abstract: Publication date: Available online 4 February 2020Source: Analytical BiochemistryAuthor(s): Wei Shen, Lei Wang, Shen Zhu, Shian Yu, Chunhui Cai, Wenjun Yi, Qing ZhuIntracellular pH plays an important role in various biological processes; abnormal pH changes in the intracellular compartment leads to the production of free radicals, the disruption of membrane contractility, inappropriate apoptosis, and necrosis, resulting in serious illness. Although fluorescent probes have widely been used to detect pH levels owing to their high sensitivity and specificity, there is still a demand for near-infrared (NIR) fluorescent probes with high Stokes shift. Here, a NIR fluorescent probe, PipDC, comprising N-ethyl piperazine (response unit) and naphthyl dicyanoisophorone (fluorophore), was designed for pH sensing. The probe has an extremely large Stokes shift (290 nm), and its fluorescence intensity at 730 nm sharply increases when the environment changes from basic to acidic owing to the protonation of piperazine, which results in the quenching of the photoinduced electron transfer effect. It exhibited a specific response to acidic microenvironments regardless of other interfering substances. In addition, PipDC operates well in the lysosome environment in living cells and displays an off-on fluorescence response with pH alterations. Together, these results suggest that PipDC is a promising fluorescent probe for intracellular pH sensing.Graphical abstractImage 1
  • Transglutaminase orthologues for medaka fish research model- biochemical
           characterization and establishment of gene-deficient mutants
    • Abstract: Publication date: Available online 31 January 2020Source: Analytical BiochemistryAuthor(s): Qi Meng, Yuko Watanabe, Risa Suzuki, Rina Oguri, Hideki Tatsukawa, Kiyotaka HitomiAbstractBy genome analysis, seven homologous genes (orthologues) of human transglutaminases (TGases) have been identified in medaka fish (Oryzias latipes), some of which clearly corresponded to the Factor XIII, TG1, and TG2. The enzymatically active-recombinant proteins for these medaka TGases has been successfully produced in bacteria or baculovirus-infected insect cell systems. Specific antibodies have been prepared and used in immunohistochemical analyses to reveal tissue distribution. Furthermore, gene-deficient medaka mutants for the genes encoding Factor XIII and TG1 have been established with analysis of their phenotypes. Retarded cross-linking of fibrin and higher sensitivity to osmolality are observed in which each gene had been knock-out. In this review, we summarize these biochemical features and the phenotypes of these gene-deficient fish.
  • Analysis of the expression of transglutaminases in the reconstructed human
           epidermis using three-dimensional cell culture
    • Abstract: Publication date: Available online 28 January 2020Source: Analytical BiochemistryAuthor(s): Hirofumi Teshima, Manami Kato, Hideki Tatsukawa, Kiyotaka HitomiAbstractThe skin epidermis functions as a barrier to various external stresses. In the outermost layer, the terminally differentiated keratinocytes result in cornification with tough structure by formation of cornified envelope beneath the plasma membrane. To complete the formation of the cornified envelope, several structural proteins are cross-linked via the catalytic action of transglutaminases (TG1, TG3, TG5, and TG6). The expression and activation of these enzymes are regulated in a tightly coordinated manner during keratinocyte differentiation. We here show the system detecting the activity of the TGases using specific glutamine-donor substrate peptides in a three-dimensional culture system of keratinocytes. In this review, we summarize the roles of the epidermal enzymes and introduce a detection method that will provide a system for evaluating the skin barrier function.
  • Nicotinamide phosphoribosyltransferase purification using SUMO expression
    • Abstract: Publication date: Available online 23 January 2020Source: Analytical BiochemistryAuthor(s): Trivikram R. Molugu, Radu C. Oita, Udeep Chawla, Sara M. Camp, Michael F. Brown, Joe G.N. GarciaNicotinamide phosphoribosyltransferase (NAMPT) is a rate-limiting enzyme in the salvage pathway required for nicotinamide adenine dinucleotide synthesis. The secreted NAMPT protein serves as a master regulatory cytokine involved in activation of evolutionarily-conserved inflammatory networks. Appreciation of the role of NAMPT as a damage-associated molecular pattern protein (DAMP) has linked its activities to several disorders via toll-like receptor 4 (TLR4) binding and inflammatory cascade activation. Information is currently lacking concerning the precise mode of the NAMPT protein functionality due to limited availability of purified protein for use in in vitro and in vivo studies. Here we report successful NAMPT expression using the pET-SUMO expression vector in E. coli strain SHuffle containing a hexa-His tag for purification. The Ulp1 protease was used to cleave the SUMO and hexa-His tags, and the protein was purified by immobilized-metal affinity chromatography. The protein yield was ∼4 mg/L and initial biophysical characterization of the protein using circular dichroism revealed the secondary structural elements, while dynamic light scattering demonstrated the presence of oligomeric units. The NAMPT-SUMO showed a predominantly dimeric protein with functional enzymatic activity. Finally, we report NAMPT solubilization in n-dodecyl-β-d-maltopyranoside (DDM) detergent in monomeric form, thus enhancing the opportunity for further structural and functional investigations.Graphical abstractImage 1
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