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Article ; Online: Analysis of polysaccharide hydrolases secreted by

Torres-Barajas, Lizzete Ruth / Alvarez-Zúñiga, María Teresa / Mendoza-Hernández, Guillermo / Aguilar-Osorio, Guillermo

Preparative biochemistry & biotechnology

2019 Volume 50, Issue 4, Page(s) 390–400

Abstract: Aspergillus ... ...

Abstract	Aspergillus flavipes
MeSH term(s)	Aspergillus/enzymology ; Aspergillus/metabolism ; Dietary Fiber ; Fungal Proteins/analysis ; Fungal Proteins/isolation & purification ; Glycoside Hydrolases/analysis ; Glycoside Hydrolases/isolation & purification ; Triticum/metabolism ; Zea mays/metabolism
Chemical Substances	Dietary Fiber ; Fungal Proteins ; Glycoside Hydrolases (EC 3.2.1.-)
Language	English
Publishing date	2019-12-12
Publishing country	England
Document type	Journal Article
ZDB-ID	1322522-4
ISSN	1532-2297 ; 1082-6068
ISSN (online)	1532-2297
ISSN	1082-6068
DOI	10.1080/10826068.2019.1700518
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Article ; Online: Impact of the vulcanization process on the structural characteristics and IgE recognition of two allergens, Hev b 2 and Hev b 6.02, extracted from latex surgical gloves.

Galicia, Christian / Mendoza-Hernández, Guillermo / Rodríguez-Romero, Adela

Molecular immunology

2015 Volume 65, Issue 2, Page(s) 250–258

Abstract: Latex allergy is a health problem that mainly affects medical environments, causing anaphylactic shocks in extreme cases. Sensitization and reactions to this material is closely linked to the use of latex gloves. The objective of this study was to purify ...

Abstract	Latex allergy is a health problem that mainly affects medical environments, causing anaphylactic shocks in extreme cases. Sensitization and reactions to this material is closely linked to the use of latex gloves. The objective of this study was to purify two of the major allergens from latex surgical gloves to study the biochemical and structural changes that could be generated during the product manufacture and to compare their IgE recognition with the non-processed allergens. Glycosylated allergen Hev b 2 (β-1,3-glucanase) and Hev b 6.02 (hevein) were purified from glove extracts using affinity (Concanavalin A) and reversed-phase chromatographies, respectively. ELISA experiments were performed with both proteins and sera from allergic patients to assess the IgE recognition, which was heterogeneous. Crystallographic methods were used to obtain the 3D structure of Hev b 6.02 from surgical gloves, which did not show evident modification when compared with the protein from the natural non-processed form. Despite having the same crystallographic structure, the IgE from some patients showed different recognition when the glove and the natural allergen were used in ELISA. Furthermore, using electrophoretic techniques, we identified three forms of Hev b 2: one corresponding to the complete polypeptide chain with posttranslational modifications, and two glycosylated fragments. The mixture of these three forms showed stronger recognition by IgE from latex-allergic patients than the pure non-processed allergen. In conclusion, IgE from subjects sensitized to latex products showed different recognition between the allergens obtained from a natural source and the processed material, even when the structure was maintained. This demonstrates the importance of using processed allergens in further investigations of diagnosis, prevalence, product allergenicity, and therapies.
MeSH term(s)	Antigens, Plant/chemistry ; Antigens, Plant/immunology ; Antigens, Plant/isolation & purification ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/immunology ; Antimicrobial Cationic Peptides/isolation & purification ; Crystallography, X-Ray ; Female ; Gloves, Surgical/adverse effects ; Hevea/chemistry ; Humans ; Immunoglobulin E/chemistry ; Immunoglobulin E/immunology ; Latex/adverse effects ; Latex/chemistry ; Latex Hypersensitivity/immunology ; Male ; Plant Lectins/chemistry ; Plant Lectins/immunology ; Plant Lectins/isolation & purification ; Plant Proteins/chemistry ; Plant Proteins/immunology ; Plant Proteins/isolation & purification ; Protein Processing, Post-Translational/immunology ; Structure-Activity Relationship
Chemical Substances	Antigens, Plant ; Antimicrobial Cationic Peptides ; Hev b 2 allergen, Hevea brasiliensis ; Latex ; Plant Lectins ; Plant Proteins ; hevein (137295-60-4) ; Immunoglobulin E (37341-29-0)
Language	English
Publishing date	2015-06
Publishing country	England
Document type	Clinical Trial ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2015.01.018
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Article ; Online: Core and accessory genome architecture in a group of Pseudomonas aeruginosa Mu-like phages.

Cazares, Adrián / Mendoza-Hernández, Guillermo / Guarneros, Gabriel

BMC genomics

2014 Volume 15, Page(s) 1146

Abstract: Background: Bacteriophages that infect the opportunistic pathogen Pseudomonas aeruginosa have been classified into several groups. One of them, which includes temperate phage particles with icosahedral heads and long flexible tails, bears genomes whose ... ...

Abstract	Background: Bacteriophages that infect the opportunistic pathogen Pseudomonas aeruginosa have been classified into several groups. One of them, which includes temperate phage particles with icosahedral heads and long flexible tails, bears genomes whose architecture and replication mechanism, but not their nucleotide sequences, are like those of coliphage Mu. By comparing the genomic sequences of this group of P. aeruginosa phages one could draw conclusions about their ontogeny and evolution. Results: Two newly isolated Mu-like phages of P. aeruginosa are described and their genomes sequenced and compared with those available in the public data banks. The genome sequences of the two phages are similar to each other and to those of a group of P. aeruginosa transposable phages. Comparing twelve of these genomes revealed a common genomic architecture in the group. Each phage genome had numerous genes with homologues in all the other genomes and a set of variable genes specific for each genome. The first group, which comprised most of the genes with assigned functions, was named "core genome", and the second group, containing mostly short ORFs without assigned functions was called "accessory genome". Like in other phage groups, variable genes are confined to specific regions in the genome. Conclusion: Based on the known and inferred functions for some of the variable genes of the phages analyzed here, they appear to confer selective advantages for the phage survival under particular host conditions. We speculate that phages have developed a mechanism for horizontally acquiring genes to incorporate them at specific loci in the genome that help phage adaptation to the selective pressures imposed by the host.
MeSH term(s)	Databases, Nucleic Acid ; Gene Order ; Genes, Viral ; Genome, Viral ; Molecular Sequence Data ; Open Reading Frames ; Phylogeny ; Pseudomonas Phages/classification ; Pseudomonas Phages/genetics ; Pseudomonas Phages/ultrastructure ; Pseudomonas aeruginosa/virology ; Sequence Homology
Language	English
Publishing date	2014-12-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1471-2164
ISSN (online)	1471-2164
DOI	10.1186/1471-2164-15-1146
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Article ; Online: The extracellular proteome of Rhizobium etli CE3 in exponential and stationary growth phase

Mendoza-Hernández Guillermo / Encarnación Sergio / Meneses Niurka

Proteome Science, Vol 8, Iss 1, p

2010 Volume 51

Abstract: Abstract Background The extracellular proteome or secretome of symbiotic bacteria like Rhizobium etli is presumed to be a key element of their infection strategy and survival. Rhizobia infect the roots of leguminous plants and establish a mutually ... ...

Abstract	Abstract Background The extracellular proteome or secretome of symbiotic bacteria like Rhizobium etli is presumed to be a key element of their infection strategy and survival. Rhizobia infect the roots of leguminous plants and establish a mutually beneficial symbiosis. To find out the possible role of secreted proteins we analyzed the extracellular proteome of R. etli CE3 in the exponential and stationary growth phases in minimal medium, supplemented with succinate-ammonium. Results The extracellular proteins were obtained by phenol extraction and identified by LC-ESI MS/MS. We identified 192 and 191 proteins for the exponential and stationary phases respectively. Using the software Signal P, we predicted signal peptides for 12.95% and 35.60% of the proteins identified in the exponential and stationary phases, respectively, which could therefore be secreted by the Sec pathway. For the exponential growth phase, we found in abundance proteins like the ribosomal proteins, toxins and proteins belonging to the group "defence mechanisms". For the stationary growth phase, we found that the most abundant proteins were those with unknown function, and in many of these we identified characteristic domains of proteases and peptidases. Conclusions Our study provided the first dataset of the secretome of R. etli and its modifications, which may lead to novel insights into the adaptive response of different stages of growth. In addition, we found a high number of proteins with unknown function; these proteins could be analyzed in future research to elucidate their role in the extracellular proteome of R. etli .
Keywords	Physiology ; QP1-981 ; Science ; Q ; DOAJ:Physiology ; DOAJ:Biology ; DOAJ:Biology and Life Sciences
Subject code	612 ; 580
Language	English
Publishing date	2010-10-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
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Article ; Online: Cor interacts with outer membrane proteins to exclude FhuA-dependent phages.

Arguijo-Hernández, Emma S / Hernandez-Sanchez, Javier / Briones-Peña, Saida J / Oviedo, Norma / Mendoza-Hernández, Guillermo / Guarneros, Gabriel / Kameyama, Luis

Archives of virology

2018 Volume 163, Issue 11, Page(s) 2959–2969

Abstract: Superinfection exclusion (Sie) of FhuA-dependent phages is carried out by Cor in the Escherichia coli mEp167 prophage lysogenic strain. In this work, we present evidence that Cor is an outer membrane (OM) lipoprotein that requires the participation of ... ...

Abstract	Superinfection exclusion (Sie) of FhuA-dependent phages is carried out by Cor in the Escherichia coli mEp167 prophage lysogenic strain. In this work, we present evidence that Cor is an outer membrane (OM) lipoprotein that requires the participation of additional outer membrane proteins (OMPs) to exclude FhuA-dependent phages. Two Cor species of ~13 and ~8.5 kDa, corresponding to the preprolipoprotein/prolipoprotein and lipoprotein, were observed by Western blot. Cell mutants for CorC17F, CorA18D and CorA57E lost the Sie phenotype for FhuA-dependent phages. A copurification affinity binding assay combined with LC_ESI_MS/MS showed that Cor bound to OMPs: OmpA, OmpC, OmpF, OmpW, LamB, and Slp. Interestingly, Sie for FhuA-dependent phages was reduced on Cor overexpressing FhuA+ mutant strains, where ompA, ompC, ompF, ompW, lamB, fhuE, genes were knocked out. The exclusion was restored when these strains were supplemented with plasmids expressing these genes. Sie was not lost in other Cor overexpressing FhuA+ null mutant strains JW3938(btuB-), JW5100(tolB-), JW3474(slp-). These results indicate that Cor interacts and requires some OMPs to exclude FhuA-dependent phages.
MeSH term(s)	Bacterial Outer Membrane Proteins/genetics ; Bacterial Outer Membrane Proteins/metabolism ; Bacteriophages/genetics ; Bacteriophages/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli/virology ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Protein Binding ; Receptors, Virus/genetics ; Receptors, Virus/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism
Chemical Substances	Bacterial Outer Membrane Proteins ; Escherichia coli Proteins ; FhuA protein, E coli ; Receptors, Virus ; Viral Proteins
Language	English
Publishing date	2018-07-24
Publishing country	Austria
Document type	Journal Article
ZDB-ID	7491-3
ISSN	1432-8798 ; 0304-8608
ISSN (online)	1432-8798
ISSN	0304-8608
DOI	10.1007/s00705-018-3954-z
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Article ; Online: The extracellular proteome of Rhizobium etli CE3 in exponential and stationary growth phase.

Meneses, Niurka / Mendoza-Hernández, Guillermo / Encarnación, Sergio

Proteome science

2010 Volume 8, Page(s) 51

Abstract: Background: The extracellular proteome or secretome of symbiotic bacteria like Rhizobium etli is presumed to be a key element of their infection strategy and survival. Rhizobia infect the roots of leguminous plants and establish a mutually beneficial ... ...

Abstract	Background: The extracellular proteome or secretome of symbiotic bacteria like Rhizobium etli is presumed to be a key element of their infection strategy and survival. Rhizobia infect the roots of leguminous plants and establish a mutually beneficial symbiosis. To find out the possible role of secreted proteins we analyzed the extracellular proteome of R. etli CE3 in the exponential and stationary growth phases in minimal medium, supplemented with succinate-ammonium. Results: The extracellular proteins were obtained by phenol extraction and identified by LC-ESI MS/MS. We identified 192 and 191 proteins for the exponential and stationary phases respectively. Using the software Signal P, we predicted signal peptides for 12.95% and 35.60% of the proteins identified in the exponential and stationary phases, respectively, which could therefore be secreted by the Sec pathway. For the exponential growth phase, we found in abundance proteins like the ribosomal proteins, toxins and proteins belonging to the group "defence mechanisms". For the stationary growth phase, we found that the most abundant proteins were those with unknown function, and in many of these we identified characteristic domains of proteases and peptidases. Conclusions: Our study provided the first dataset of the secretome of R. etli and its modifications, which may lead to novel insights into the adaptive response of different stages of growth. In addition, we found a high number of proteins with unknown function; these proteins could be analyzed in future research to elucidate their role in the extracellular proteome of R. etli.
Language	English
Publishing date	2010-10-14
Publishing country	England
Document type	Journal Article
ISSN	1477-5956
ISSN (online)	1477-5956
DOI	10.1186/1477-5956-8-51
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Article: Structural and kinetics characterization of the F

Esparza-Perusquía, Mercedes / Olvera-Sánchez, Sofía / Pardo, Juan Pablo / Mendoza-Hernández, Guillermo / Martínez, Federico / Flores-Herrera, Oscar

Biochimica et biophysica acta. Bioenergetics

2017 Volume 1858, Issue 12, Page(s) 975–981

Abstract: Ustilago maydis is an aerobic basidiomycete that fully depends on oxidative phosphorylation for its supply of ATP, pointing to mitochondria as a key player in the energy metabolism of this organism. Mitochondrial ... ...

Abstract	Ustilago maydis is an aerobic basidiomycete that fully depends on oxidative phosphorylation for its supply of ATP, pointing to mitochondria as a key player in the energy metabolism of this organism. Mitochondrial F
MeSH term(s)	Adenosine Triphosphate/chemistry ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence/genetics ; Energy Metabolism/genetics ; Hydrolysis/drug effects ; Kinetics ; Mass Spectrometry ; Mitochondria/enzymology ; Mitochondrial Proton-Translocating ATPases/chemistry ; Mitochondrial Proton-Translocating ATPases/genetics ; Mitochondrial Proton-Translocating ATPases/metabolism ; Oligomycins/pharmacology ; Protein Multimerization/genetics ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Ustilago/enzymology
Chemical Substances	Oligomycins ; Protein Subunits ; Adenosine Triphosphate (8L70Q75FXE) ; F1F0-ATP synthase (EC 3.6.1.-) ; Mitochondrial Proton-Translocating ATPases (EC 3.6.3.-)
Language	English
Publishing date	2017-09-14
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0005-2728 ; 0006-3002 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0005-2728 ; 0006-3002 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2017.09.002
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Article ; Online: Comparative genomic analysis of two brucellaphages of distant origins.

Flores, Victor / López-Merino, Ahidé / Mendoza-Hernandez, Guillermo / Guarneros, Gabriel

Genomics

2012 Volume 99, Issue 4, Page(s) 233–240

Abstract: Here, we present the first complete genome sequence of brucellaphage Tbilisi (Tb) and compared it with that of Pr, a broad host-range brucellaphage recently isolated in Mexico. The genomes consist of 41,148 bp (Tb) and 38,253 bp (Pr), they differ mainly ... ...

Abstract	Here, we present the first complete genome sequence of brucellaphage Tbilisi (Tb) and compared it with that of Pr, a broad host-range brucellaphage recently isolated in Mexico. The genomes consist of 41,148 bp (Tb) and 38,253 bp (Pr), they differ mainly in the region encoding structural proteins, in which the genome of Tb shows two major insertions. Both genomes share 99.87% nucleotide identity, a high percentage of identity among phages isolated at so globally distant locations and temporally different occasions. Sequence analysis revealed 57 conserved ORFs, three transcriptional terminators and four putative transcriptional promoters. The co-occurrence of an ORF encoding a putative DnaA-like protein and a putative oriC-like origin of replication was found in both brucellaphages genomes, a feature not described in any other phage genome. These elements suggest that DNA replication in brucellaphages differs from other phages, and might resemble that of bacterial chromosomes.
MeSH term(s)	Bacteriophages/genetics ; Brucella/isolation & purification ; Brucella/virology ; Chromosomes, Bacterial/genetics ; Computational Biology/methods ; DNA Primers/genetics ; DNA Primers/metabolism ; DNA Replication ; DNA, Bacterial/genetics ; DNA, Bacterial/isolation & purification ; Genome, Viral ; Mexico ; Molecular Sequence Data ; Open Reading Frames ; Polymorphism, Single Nucleotide ; Proteomics ; Sequence Analysis, DNA ; Transcription, Genetic
Chemical Substances	DNA Primers ; DNA, Bacterial
Language	English
Publishing date	2012-04
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	356334-0
ISSN	1089-8646 ; 0888-7543
ISSN (online)	1089-8646
ISSN	0888-7543
DOI	10.1016/j.ygeno.2012.01.001
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Article ; Online: Purification, properties, and kinetic studies of cytoplasmic malate dehydrogenase from Taenia solium cysticerci.

Plancarte, Agustín / Nava, Gabriela / Mendoza-Hernández, Guillermo

Parasitology research

2009 Volume 105, Issue 1, Page(s) 175–183

Abstract: Malate dehydrogenase (L: -malate: NAD oxidoreductase, EC 1.1.1.37) from the cytoplasm of Taenia solium cysticerci (cMDHTs) was purified 48-fold through a four-step procedure involving salt fractionation, ionic exchange, and dye affinity chromatography. ... ...

Abstract	Malate dehydrogenase (L: -malate: NAD oxidoreductase, EC 1.1.1.37) from the cytoplasm of Taenia solium cysticerci (cMDHTs) was purified 48-fold through a four-step procedure involving salt fractionation, ionic exchange, and dye affinity chromatography. cMDHTs had a native M (r) of 64,000, while the corresponding value per subunit, obtained under denaturing conditions, was 32,000. The enzyme is partially positive, with an isoelectric point of 8.7, and had a specific activity of 2,615 U mg(-1) in the reduction of oxaloacetate. The second to the 21st amino acids from cMDHTs N-terminal group were P G P L R V L I T G A A G Q I A Y N L S. This sequence is 100% identical to that of Echinococcus granulosus. Basic kinetic parameters were determined for this enzyme. The optimum pH for enzyme reaction was at 7.6 for oxaloacetate reduction and at 9.6 for malate oxidation. K (m) values for oxaloacetate, malate, NAD, and NADH were 2.4, 215, 50, and 48 microM, respectively. V (max) values for the substrates and cosubstrates as described above were 1,490, 87.8, 104, and 1,714 micromol min(-1) mg(-1). Several NAD analogs, structurally altered in either the pyridine or purine moiety, were observed to function as coenzymes in the reaction catalyzed by the purified malate dehydrogenase. cMDHTs activity was uncompetitive inhibited by arsenate for both the forward (Ki = 8.2 mM) and reverse (Ki = 77 mM) reactions. The mechanism of the cMDHTs reactivity was investigated kinetically by the product inhibition approach. The results of this study are qualitatively consistent with an Ordered Bi Bi reaction mechanism, in which only the coenzymes can react with the free enzyme.
MeSH term(s)	Animals ; Arsenates/pharmacology ; Chemical Fractionation ; Chromatography, Affinity ; Chromatography, Ion Exchange ; Coenzymes/pharmacology ; Cytoplasm/enzymology ; Echinococcus granulosus/genetics ; Enzyme Inhibitors/pharmacology ; Helminth Proteins/chemistry ; Helminth Proteins/isolation & purification ; Helminth Proteins/metabolism ; Hydrogen-Ion Concentration ; Isoelectric Point ; Kinetics ; Malate Dehydrogenase/chemistry ; Malate Dehydrogenase/isolation & purification ; Malate Dehydrogenase/metabolism ; Malates/metabolism ; Molecular Weight ; NAD/pharmacology ; Oxaloacetic Acid/metabolism ; Protein Subunits ; Sequence Analysis, Protein ; Sequence Homology, Amino Acid ; Taenia solium/enzymology
Chemical Substances	Arsenates ; Coenzymes ; Enzyme Inhibitors ; Helminth Proteins ; Malates ; Protein Subunits ; NAD (0U46U6E8UK) ; Oxaloacetic Acid (2F399MM81J) ; malic acid (817L1N4CKP) ; Malate Dehydrogenase (EC 1.1.1.37) ; arsenic acid (N7CIZ75ZPN)
Language	English
Publishing date	2009-03-10
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	284966-5
ISSN	1432-1955 ; 0932-0113 ; 0044-3255
ISSN (online)	1432-1955
ISSN	0932-0113 ; 0044-3255
DOI	10.1007/s00436-009-1380-6
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Article: Purification, properties, and kinetic studies of cytoplasmic malate dehydrogenase from Taenia solium cysticerci

Plancarte, Agustín / Nava, Gabriela / Mendoza-Hernández, Guillermo

Parasitology research. 2009 June, v. 105, no. 1

2009

Abstract: Malate dehydrogenase (l-malate: NAD oxidoreductase, EC 1.1.1.37) from the cytoplasm of Taenia solium cysticerci (cMDHTs) was purified 48-fold through a four-step procedure involving salt fractionation, ionic exchange, and dye affinity chromatography. ... ...

Abstract	Malate dehydrogenase (l-malate: NAD oxidoreductase, EC 1.1.1.37) from the cytoplasm of Taenia solium cysticerci (cMDHTs) was purified 48-fold through a four-step procedure involving salt fractionation, ionic exchange, and dye affinity chromatography. cMDHTs had a native M r of 64,000, while the corresponding value per subunit, obtained under denaturing conditions, was 32,000. The enzyme is partially positive, with an isoelectric point of 8.7, and had a specific activity of 2,615 U mg⁻¹ in the reduction of oxaloacetate. The second to the 21st amino acids from cMDHTs N-terminal group were P G P L R V L I T G A A G Q I A Y N L S. This sequence is 100% identical to that of Echinococcus granulosus. Basic kinetic parameters were determined for this enzyme. The optimum pH for enzyme reaction was at 7.6 for oxaloacetate reduction and at 9.6 for malate oxidation. K m values for oxaloacetate, malate, NAD, and NADH were 2.4, 215, 50, and 48 μM, respectively. V max values for the substrates and cosubstrates as described above were 1,490, 87.8, 104, and 1,714 μmol min⁻¹ mg⁻¹. Several NAD analogs, structurally altered in either the pyridine or purine moiety, were observed to function as coenzymes in the reaction catalyzed by the purified malate dehydrogenase. cMDHTs activity was uncompetitive inhibited by arsenate for both the forward (Ki = 8.2 mM) and reverse (Ki = 77 mM) reactions. The mechanism of the cMDHTs reactivity was investigated kinetically by the product inhibition approach. The results of this study are qualitatively consistent with an Ordered Bi Bi reaction mechanism, in which only the coenzymes can react with the free enzyme.
Keywords	Echinococcus granulosus ; NAD (coenzyme) ; Taenia solium ; affinity chromatography ; amino acids ; cysticerci ; cytoplasm ; dyes ; fractionation ; isoelectric point ; malate dehydrogenase ; malates ; oxidation ; pH
Language	English
Dates of publication	2009-06
Size	p. 175-183.
Publisher	Springer-Verlag
Publishing place	Berlin/Heidelberg
Document type	Article
ZDB-ID	284966-5
ISSN	1432-1955 ; 0932-0113 ; 0044-3255
ISSN (online)	1432-1955
ISSN	0932-0113 ; 0044-3255
DOI	10.1007/s00436-009-1380-6
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