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1.
Prikl Biokhim Mikrobiol ; 52(2): 193-9, 2016.
Artigo em Russo | MEDLINE | ID: mdl-27266248

RESUMO

A system for the production of mutant recombinant human alpha-fetoprotein (rhAFPO) lacking the glycosylation site has been engineered in the yeast Pichia pastoris. A strain of the methylotrophic yeast Pichia pastoris GS 115/pPICZ?A/rhAFP0, which produces unglycosylated rhAFPO and secretes it to the culture medium, has been constructed. Optimization and scale-up of the fermentation technology have resulted in an increase in the rhAFP0 yield to 20 mg/L. A scheme of isolation and purification of biologically active rhAFP0 has been developed. The synthesized protein has the antitumor activity, which is analogous to the activity of natural human embryonic alpha-fetoprotein.


Assuntos
Proteínas Mutantes/biossíntese , Neoplasias/tratamento farmacológico , Proteínas Recombinantes/biossíntese , alfa-Fetoproteínas/biossíntese , Linhagem Celular Tumoral , Fermentação , Humanos , Proteínas Mutantes/administração & dosagem , Proteínas Mutantes/genética , Pichia/genética , Proteínas Recombinantes/administração & dosagem , Proteínas Recombinantes/genética , Proteínas Recombinantes/isolamento & purificação , Saccharomyces cerevisiae/genética , alfa-Fetoproteínas/administração & dosagem , alfa-Fetoproteínas/genética , alfa-Fetoproteínas/isolamento & purificação
2.
Biochemistry (Mosc) ; 77(10): 1190-8, 2012 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-23157299

RESUMO

The gene xylE encoding endo-1,4-ß-xylanase from the 10th family of glycosyl hydrolases produced by the mycelial fungus Penicillium canescens has been expressed under the control of the strong promoter of the bgaS gene encoding ß-galactosidase from P. canescens. As a result, a strain-producer of endoxylanase XylE was developed. The recombinant enzyme was isolated and purified to homogeneity with specific activity of 50 U/mg. The physicochemical and biochemical properties of the endoxylanase were studied. The maximal enzymatic activity was observed at pH 6.0 and 70°C. Endoxylanase XylE was shown to be a highly thermostable enzyme with half-inactivation period τ(1/2) of 7 h at 60°C. The kinetic parameters were 0.52 mg/ml (K(m)) and 75 µmol/min per mg (V(max)) using birch xylan as the substrate. Crystals of endoxylonase XylE were obtained, and the 3D structure was solved at 1.47 Å resolution. The 3D structure of an endo-1,4-ß-xylanase from the 10th family containing carbohydrate and unique cyclic structure located at the C-terminus of the polypeptide chain was obtained for the first time.


Assuntos
Endo-1,4-beta-Xilanases/genética , Endo-1,4-beta-Xilanases/metabolismo , Proteínas de Escherichia coli/química , Proteínas de Escherichia coli/metabolismo , Penicillium/enzimologia , Penicillium/genética , Proteínas Recombinantes/metabolismo , Simportadores/química , Simportadores/metabolismo , Cristalografia por Raios X , Endo-1,4-beta-Xilanases/química , Endo-1,4-beta-Xilanases/isolamento & purificação , Proteínas de Escherichia coli/genética , Proteínas Recombinantes/genética , Especificidade por Substrato , Simportadores/genética
3.
Genetika ; 47(2): 174-82, 2011 Feb.
Artigo em Russo | MEDLINE | ID: mdl-21516789

RESUMO

Four novel genes of the enzymes of the endoxylanase (EC 3.2.1.8) families found in the mycelial fungus Penicillium canescens have been cloned. The xylB, xylC, and xylD genes encode endoxylanases of glycosyl hydrolase family 11; the xylEgene, those of family 10. In the promoter region of the xylB, xylC, and xylD genes, the binding sequences for the protein activator of xylanolytic gene transcription have been found; the promoter region of the xylB gene contains the binding sequences for the catabolite repression protein. Since the TATAA sequence, which is an element of the minimal eukaryotic promoter, has not been found in the promoter region of the xylC gene, in contrast to those of the xylB and xylD genes, it may be assumed that this gene is silent. Comparative phylogenetic analysis has shown that the cloned genes are highly homologous to some endoxylanase genes of mycelial fungi of the genera Penicillium and Aspergillus. However, within the species P. canescens, they exhibit a low homology both within and between families, and they diverge into different branches of the phylogenetic tree, which suggest divergence of the genes of this group at an early stage of evolution.


Assuntos
Endo-1,4-beta-Xilanases/genética , Proteínas Fúngicas/genética , Genes Fúngicos/fisiologia , Família Multigênica/fisiologia , Penicillium/genética , Proteínas Repressoras/genética , Aspergillus/enzimologia , Aspergillus/genética , Endo-1,4-beta-Xilanases/metabolismo , Proteínas Fúngicas/metabolismo , Penicillium/enzimologia , Filogenia , Proteínas Repressoras/metabolismo , Elementos de Resposta/fisiologia , Homologia de Sequência de Aminoácidos , Transcrição Gênica/fisiologia
4.
Mol Biol (Mosk) ; 45(5): 871-8, 2011.
Artigo em Russo | MEDLINE | ID: mdl-22393784

RESUMO

Penicillium canescens strain F178 is a natural producer of beta-galactosidase and endo-1,4-beta-xylanase. The transcription of genes bgaS and xylA, coding for these proteins, is subject to carbon catabolite repression. The system for selective isolation of regulatory mutants in P. canescens is developed. Two strains from the mutant collection are studied in details. It is shown that both mutations can be complement by creA gene of P. canescens, encoding global regulator of carbon catabolite repression in filamentous fungi. creA(-) alleles contain frameshift mutations in C-domain of CreA. Gene xylA is derepressed in mutants at transcription level in the presence of D-glucose. A transcription of creA gene in mutants is also derepressed proving effect of autoregulation for this gene.


Assuntos
Repressão Catabólica/genética , Endo-1,4-beta-Xilanases/metabolismo , Regulação Fúngica da Expressão Gênica , Penicillium/genética , Proteínas Repressoras/metabolismo , beta-Galactosidase/metabolismo , Alelos , Sequência de Aminoácidos , Repressão Catabólica/efeitos dos fármacos , Repressão Catabólica/efeitos da radiação , Análise Mutacional de DNA , Endo-1,4-beta-Xilanases/genética , Mutação da Fase de Leitura , Proteínas Fúngicas/genética , Proteínas Fúngicas/metabolismo , Regulação Fúngica da Expressão Gênica/efeitos dos fármacos , Regulação Fúngica da Expressão Gênica/efeitos da radiação , Glucose/metabolismo , Glucose/farmacologia , Dados de Sequência Molecular , Penicillium/efeitos dos fármacos , Penicillium/enzimologia , Penicillium/efeitos da radiação , Plasmídeos , Reação em Cadeia da Polimerase em Tempo Real , Proteínas Repressoras/genética , Seleção Genética , Alinhamento de Sequência , Transcrição Gênica/efeitos dos fármacos , Transcrição Gênica/efeitos da radiação , Raios Ultravioleta , beta-Galactosidase/genética
5.
Mol Biol (Mosk) ; 44(4): 677-87, 2010.
Artigo em Russo | MEDLINE | ID: mdl-20873228

RESUMO

Penicillium canescens strain F178 is a natural producer of beta-galactosidase and endo-1,4-beta-xylanase. Tanscription of genes bgaS and xylA coding for these proteins is subject to carbon catabolite repression which proceed mainly in filamentous fungi by transcriptional repressor CreA. creA gene of P. canescens was cloned. It was demonstrated that creA transcription is also subject to carbon catabolite repression. CreA protein remains intranuclear independently of nature of carbon source and glucose concentration in culture medium. In vitro experiments confirm availability of four CreA-binding sites in bgaS promoter, four sites in xylA promoter and one such site in creA promoter.


Assuntos
Carbono/metabolismo , Proteínas Fúngicas/metabolismo , Regulação Fúngica da Expressão Gênica/fisiologia , Penicillium/metabolismo , Proteínas Repressoras/metabolismo , Transcrição Gênica/fisiologia , Endo-1,4-beta-Xilanases/biossíntese , Endo-1,4-beta-Xilanases/genética , Proteínas Fúngicas/genética , Regulação Enzimológica da Expressão Gênica/fisiologia , Penicillium/genética , Proteínas Repressoras/genética , beta-Galactosidase/biossíntese , beta-Galactosidase/genética
6.
Prikl Biokhim Mikrobiol ; 46(3): 342-7, 2010.
Artigo em Russo | MEDLINE | ID: mdl-20586288

RESUMO

A heterologous protein expression in the fungus Penicillium canescens is described for the first time. The fungal strains producing Trametes hirsuta laccase under control of a highly efficient promoter of the P. canescens gene bgaS has been constructed. These strains efficiently transcribe the T. hirsuta 072 laccase gene with a correct intron splicing. Activity of the secreted heterologous laccase in the culture liquid reaches 3 U/ml, accounting for 98% of the total laccase activity, which demonstrates a high efficiency ofheterologous secretion. The synthesized P. canescens laccase has the same molecular weight as the enzyme produced by T. hirsuta 072.


Assuntos
Proteínas Fúngicas/biossíntese , Expressão Gênica , Penicillium/crescimento & desenvolvimento , Proteínas Recombinantes/biossíntese , Trametes/enzimologia , Proteínas Fúngicas/genética , Lacase , Penicillium/genética , Regiões Promotoras Genéticas/genética , Proteínas Recombinantes/genética , Trametes/genética
7.
Biochemistry (Mosc) ; 74(8): 882-7, 2009 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-19817688

RESUMO

The gene encoding the xlnR xylanolytic activator of the heterologous fungus Aspergillus niger was incorporated into the Penicillium canescens genome. Integration of the xlnR gene resulted in the increase in a number of activities, i.e. endoxylanase, beta-xylosidase, alpha-L-arabinofuranosidase, alpha-galactosidase, and feruloyl esterase, compared to the host P. canescens PCA 10 strain, while beta-galactosidase, beta-glucosidase, endoglucanase, and CMCase activities remained constant. Two different expression constructs were developed. The first consisted of the nucleotide sequence containing the mature P. canescens phytase gene under control of the axhA promoter region gene encoding A. niger (1,4)-beta-D-arabinoxylan-arabinofuranohydrolase. The second construct combined the P. canescens phytase gene and the bgaS promoter region encoding homologous beta-galactosidase. Both expression cassettes were transformed into P. canescens host strain containing xlnR. Phytase synthesis was observed only for strains with the bgaS promoter on arabinose-containing culture media. In conclusion, the bgaS and axhA promoters were regulated by different inducers and activators in the P. canescens strain containing a structural tandem of the axhA promoter and the gene of the xlnR xylanolytic activator.


Assuntos
Proteínas Fúngicas/metabolismo , Regulação Fúngica da Expressão Gênica , Genes Reguladores , Penicillium/genética , Transativadores/metabolismo , Celulase/genética , Celulase/metabolismo , Proteínas Fúngicas/genética , Regulação Enzimológica da Expressão Gênica , Engenharia Genética , Glicosídeo Hidrolases/genética , Glicosídeo Hidrolases/metabolismo , Penicillium/enzimologia , Penicillium/metabolismo , Regiões Promotoras Genéticas , Transativadores/genética , alfa-Galactosidase/genética , alfa-Galactosidase/metabolismo , beta-Galactosidase/genética , beta-Galactosidase/metabolismo , beta-Glucosidase/genética , beta-Glucosidase/metabolismo
8.
Biochemistry (Mosc) ; 74(6): 655-62, 2009 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-19645671

RESUMO

Gene egl2 of secreted endo-(1-4)-beta-glucanase of glycosyl hydrolase family 5 of the mycelial fungus Penicillium canescens was cloned. The gene was expressed in P. canescens under control of a strong promoter of the bgaS gene encoding beta-galactosidase of P. canescens, and endoglucanase producing strains were obtained. Chromatographically purified recombinant 48 kDa protein had pH and temperature optima 3.4 and 60 degrees C, respectively, exhibited specific activity of 33 IU, and had K(m) and V(max) in CM-cellulose hydrolysis of 10.28 g/liter and 0.26 micromol/sec per mg, respectively.


Assuntos
Celulase/genética , Celulase/metabolismo , Proteínas Fúngicas/metabolismo , Genes Fúngicos , Penicillium/enzimologia , Sequência de Aminoácidos , Sequência de Bases , Varredura Diferencial de Calorimetria , Carboximetilcelulose Sódica/metabolismo , Celulase/biossíntese , Celulase/isolamento & purificação , Estabilidade Enzimática , Escherichia coli/genética , Proteínas Fúngicas/biossíntese , Proteínas Fúngicas/genética , Proteínas Fúngicas/isolamento & purificação , Galactosidases/genética , Galactosidases/metabolismo , Temperatura Alta , Concentração de Íons de Hidrogênio , Cinética , Dados de Sequência Molecular , Nitrato Redutase/genética , Nitrato Redutase/metabolismo , Sinais Direcionadores de Proteínas , Proteínas Recombinantes/metabolismo , Alinhamento de Sequência , Transformação Bacteriana
9.
Prikl Biokhim Mikrobiol ; 45(2): 163-70, 2009.
Artigo em Russo | MEDLINE | ID: mdl-19382702

RESUMO

The gene egl3 of the filamentous fungus Penicillium canescens endo-1,4-beta-glucanase, belonging to family 12 glycosyl hydrolases, was cloned and sequenced. The gene was expressed in P. canescens under the control of the strong promoter of gene bgaS, coding for beta-galactosidase of this fungus, and efficient endoglucanase producer strains were obtained. The recombinant protein was isolated from the culture liquid of the producer strain EGL3-13 and purified to homogeneity; its specific activity was 31.7 IU; molecular weight, 26 kDa; and pH and temperature optimums, 3.2 and 54 degrees C, respectively. The Km and Vm values for CMC hydrolysis were determined; they amounted to 17.1 g/1 and 0.31 microM/(mg s), respectively.


Assuntos
Celulase/biossíntese , Celulase/química , Proteínas Fúngicas/biossíntese , Proteínas Fúngicas/química , Penicillium/enzimologia , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/química , Celulase/genética , Celulase/isolamento & purificação , Clonagem Molecular/métodos , Proteínas Fúngicas/isolamento & purificação , Expressão Gênica , Temperatura Alta , Concentração de Íons de Hidrogênio , Cinética , Penicillium/genética , Proteínas Recombinantes/genética , Proteínas Recombinantes/isolamento & purificação
10.
Biochemistry (Mosc) ; 73(1): 97-106, 2008 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-18294137

RESUMO

Two alpha-galactosidases were purified to homogeneity from the enzymatic complex of the mycelial fungus Penicillium canescens using chromatography on different sorbents. Substrate specificity, pH- and temperature optima of activity, stability under different pH and temperature conditions, and the influence of effectors on the catalytic properties of both enzymes were investigated. Genes aglA and aglC encoding alpha-galactosidases from P. canescens were isolated, and amino acid sequences of the proteins were predicted. In vitro feed testing (with soybean meal and soybean byproducts enriched with galactooligosaccharides as substrates) demonstrated that both alpha-galactosidases from P. canescens could be successfully used as feed additives. alpha-Galactosidase A belonging to the 27th glycosyl hydrolase family hydrolyzed galactopolysaccharides (galactomannans) and alpha-galactosidase C belonging to the 36th glycosyl hydrolase family hydrolyzed galactooligosaccharides (stachyose, raffinose, etc.) of soybean with good efficiency, thus improving the digestibility of fodder.


Assuntos
Proteínas Fúngicas/química , Penicillium/enzimologia , alfa-Galactosidase/química , Ração Animal , Animais , Cátions Bivalentes/química , Estabilidade Enzimática , Proteínas Fúngicas/isolamento & purificação , Proteínas Fúngicas/metabolismo , Galactose/química , Concentração de Íons de Hidrogênio , Cinética , Metais/química , Homologia de Sequência de Aminoácidos , Especificidade por Substrato , Temperatura , alfa-Galactosidase/isolamento & purificação , alfa-Galactosidase/metabolismo
11.
Biochemistry (Mosc) ; 72(5): 565-71, 2007 May.
Artigo em Inglês | MEDLINE | ID: mdl-17573712

RESUMO

Pectin lyase A (molecular weight 38 kD by SDS-PAGE, pI 6.7) was purified to homogeneity from culture broth of the mycelial fungus Penicillium canescens using chromatographic techniques. During genomic library screening, the gene encoding pectin lyase A from P. canescens (pelA) was isolated and sequenced, and the amino acid sequence was generated by applying the multiple alignment procedure (360 residues). A theoretical model for the three dimensional structure of the protein molecule was also proposed. Different properties of pectin lyase A were investigated: substrate specificity, pH- and temperature optimum of activity, stability under different pH and temperature conditions, and the effect of Ca2+ on enzyme activity. In the course of the laboratory trials, it was demonstrated that pectin lyase A from P. canescens could be successfully applied to production and clarification of juice.


Assuntos
Espaço Extracelular/enzimologia , Proteínas Fúngicas/química , Penicillium/enzimologia , Polissacarídeo-Liases/isolamento & purificação , Polissacarídeo-Liases/metabolismo , Sequência de Aminoácidos , Bebidas , Cálcio/farmacologia , Cromatografia por Troca Iônica , DNA Fúngico/química , DNA Fúngico/genética , Eletroforese em Gel de Poliacrilamida , Estabilidade Enzimática , Frutas/enzimologia , Frutas/metabolismo , Proteínas Fúngicas/genética , Concentração de Íons de Hidrogênio , Hidrólise/efeitos dos fármacos , Focalização Isoelétrica , Dados de Sequência Molecular , Pectinas/metabolismo , Penicillium/genética , Polissacarídeo-Liases/genética , Conformação Proteica , Alinhamento de Sequência , Análise de Sequência de DNA , Análise de Sequência de Proteína , Homologia de Sequência de Aminoácidos , Especificidade por Substrato , Temperatura
12.
Prikl Biokhim Mikrobiol ; 38(5): 495-501, 2002.
Artigo em Russo | MEDLINE | ID: mdl-12391748

RESUMO

The complete gene xylA that encodes endo-1,4-beta-xylanase secreted by Penicillium canescens was cloned and sequenced. The coding region of the gene is separated by eight introns. The protein comprises 302 amino acids of the mature protein and 25 amino acids of the signal peptide. The xylanase of P. canescens belongs to the glycosyl hydrolase family 10. Nucleotide sequences for binding catabolite repression protein CREA and transactivator protein were detected in the promoter region. A set of multicopy strains displaying a seven-eightfold increase in xylanase yield was obtained. The fraction of xylanase in most productive strains amounted to 30-50% of the total secreted protein.


Assuntos
Genes Fúngicos , Penicillium/enzimologia , Xilosidases/genética , Sequência de Aminoácidos , Sequência de Bases , Clonagem Molecular , DNA Fúngico , Eletroforese em Gel de Poliacrilamida , Endo-1,4-beta-Xilanases , Concentração de Íons de Hidrogênio , Dados de Sequência Molecular , Homologia de Sequência de Aminoácidos , Temperatura , Transativadores/metabolismo , Xilosidases/metabolismo
13.
Isr Med Assoc J ; 2 Suppl: 92-8, 2000 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-10909425

RESUMO

P2-receptors (P2-Rs) represent significant targets for novel drug development. P2-Rs were identified also on pancreatic B cells and are involved in insulin secretion. The aim of our study was to synthesize and evaluate pharmacologically the novel P2Y-R ligands, 2-thioether-5'-O-phosphorothioate adenosine derivatives, as potential insulin secretagogues. An efficient synthesis of these nucleosides and a facile method for separation of the chiral products is described. The enzymatic stability of the compounds towards pig-pancreas NTPDase was evaluated. The rate of hydrolysis of 2-hexylthio-5'-O-(1-thiotriphosphate)-adenosine (2-hexylthio-ATP-alpha-S) isomers by NTPDase was 28% that of ATP. The apparent affinity of the compounds to P2Y1-R was determined by measurement of P2Y-receptor-promoted phospholipase C activity in turkey erythrocyte membranes. 2-RS-ATP-alpha-S derivatives were agonists, stimulating the production of inositol phosphates with K0.5 values in the nM range. 2-RS-AMP-S derivatives were full agonists although 2 orders of magnitude less potent. All the compounds were more potent than ATP. The effect on insulin secretion and pancreatic flow rate was evaluated on isolated and perfused rat pancreas. A high increase, up to 500%, in glucose-induced insulin secretion was due to addition of 2-hexylthio-ATP-alpha-S in the nM concentration range, which represents 100-fold enhancement of activity relative to ATP. 2-Hexylthio-AMP-S was 2.5 orders of magnitude less effective. A high chemical hydrolytic stability was observed for 2-hexylthio-ATP-alpha-S. Hydrolysis of the phosphoester bond, which was the only detectable degrading reaction under the investigation conditions (pH 7.4, 37 degrees C), was slow, with a half-life of 264 hours. Moreover, even at gastric juice conditions (pH 1.4, 37 degrees C), hydrolysis of the terminal phosphate was the only detectable reaction, with a half-life of 17.5 hours. 2-Hexylthio-ATP-alpha-S isomers are enzymatically and chemically stable. These isomers are highly potent and effective insulin secretagogues, increasing, however, pancreatic vascular resistance.


Assuntos
Nucleotídeos de Adenina/farmacologia , Adenosina/análogos & derivados , Adenosina/farmacologia , Insulina/metabolismo , Receptores Purinérgicos P2/efeitos dos fármacos , Sulfetos/farmacologia , Tionucleotídeos/farmacologia , Hidrolases Anidrido Ácido/metabolismo , Nucleotídeos de Adenina/metabolismo , Adenosina/metabolismo , Animais , Desenho de Fármacos , Eritrócitos/enzimologia , Glucose/farmacologia , Meia-Vida , Concentração de Íons de Hidrogênio , Hidrólise , Fosfatos de Inositol/biossíntese , Secreção de Insulina , Ilhotas Pancreáticas/efeitos dos fármacos , Isomerismo , Ligantes , Nucleosídeo-Trifosfatase , Pâncreas/irrigação sanguínea , Pâncreas/enzimologia , Ratos , Taxa Secretória/efeitos dos fármacos , Sulfetos/metabolismo , Suínos , Tionucleotídeos/metabolismo , Perus , Fosfolipases Tipo C/metabolismo , Resistência Vascular/efeitos dos fármacos
14.
J Med Chem ; 42(18): 3636-46, 1999 Sep 09.
Artigo em Inglês | MEDLINE | ID: mdl-10479295

RESUMO

P2-Receptors (P2-Rs) represent significant targets for novel drug development. P2-Rs were identified also on pancreatic B cells and are involved in insulin secretion. Therefore, novel P2Y-R ligands, 2-thioether 5'-O-phosphorothioate adenosine derivatives (2-RS-ATP-alpha-S), were synthesized as potential insulin secretagogues. An efficient synthesis of these nucleotides and a facile method for separation of the chiral products are described. The enzymatic stability of the compounds toward pig pancreas type I ATPDase was evaluated. The rate of hydrolysis of 2-hexylthio-5'-O-(1-thiotriphosphate)adenosine (2-hexylthio-ATP-alpha-S) isomers by ATPDase was 28% of that of ATP. Some 2-thioether 5'-(monophosphorothioate)adenosine derivatives (2-RS-AMP-S) exerted an inhibitory effect on ATPDase. The apparent affinity of the compounds to P2Y(1)-R was determined by measurement of P2Y-R-promoted phospholipase C activity in turkey erythrocyte membranes. 2-RS-ATP-alpha-S derivatives were agonists, stimulating the production of inositol phosphates with K(0.5) values in the nanomolar range. 2-RS-AMP-S derivatives were full agonists, although 2 orders of magnitude less potent. All the compounds were more potent than ATP. The effect on insulin secretion and pancreatic flow rate was evaluated on isolated and perfused rat pancreas. A high increase, up to 500%, in glucose-induced insulin secretion was due to addition of 2-hexylthio-ATP-alpha-S in the nanomolar concentration range, which represents 100-fold enhancement of activity relative to ATP. 2-Hexylthio-AMP-S was 2.5 orders of magnitude less effective.


Assuntos
Trifosfato de Adenosina/análogos & derivados , Insulina/metabolismo , Pâncreas/efeitos dos fármacos , Agonistas do Receptor Purinérgico P2 , Tionucleotídeos/química , Adenosina/análogos & derivados , Trifosfato de Adenosina/metabolismo , Animais , Apirase/metabolismo , Estabilidade Enzimática , Secreção de Insulina , Ilhotas Pancreáticas/efeitos dos fármacos , Ilhotas Pancreáticas/metabolismo , Cinética , Nucleotídeos/síntese química , Nucleotídeos/farmacologia , Pâncreas/enzimologia , Sulfetos/síntese química , Sulfetos/farmacologia , Suínos
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