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1.
Bioorg Khim ; 27(5): 347-51, 2001.
Artigo em Russo | MEDLINE | ID: mdl-11641908

RESUMO

The segment condensation of peptides on a solid phase (Aminosilochrom) in organic medium catalyzed by a subtilisin complex with sodium dodecylsulfate was studied. The dependence of the efficiency of the enzymatic coupling of tripeptides with the basic structure X-Ala-Ala-Y-OMe [where X = Z, Boc, or Dnp and Y = Leu or Glu(OMe)] on the spacer content on the support and on the structure of the acylating component was investigated. The tripeptide segments were successively coupled to Aminosilochrom containing the Met-Ala-Gly spacer, and the peptidylaminosilochroms Dnp-Ala-Ala-Leu-Ala-Ala-Leu-Ala-Ala-Glu(OMe)-Met-Ala-Gly-A and Dnp-Ala-Ala-Leu-Ala-Ala-Glu(OMe)-Ala-Ala-Leu-Met-Ala-Gly-A (A is the Aminosilochrom residue) were obtained in satisfactory yields. It was shown by these examples that the second and third segments are attached in yields higher than that for the first segment and the coupling efficiency does not depend on the amino acid composition of the acylating component.


Assuntos
Peptídeos/síntese química , Dióxido de Silício , Aminoácidos , Peptídeos/química
2.
Bioorg Khim ; 26(6): 411-6, 2000 Jun.
Artigo em Russo | MEDLINE | ID: mdl-10923188

RESUMO

The subtilisin-sodium dodecyl sulfate complex was shown to catalyze the coupling of peptide segments on a solid phase in organic medium. By a two-stage enzymic condensation of peptide fragments on aminosilochrom (A) containing Met-Ala-Gly as a spacer, Dnp(or Boc)-Ala-Ala-Leu-Ala-Ala-Glu(OMe)-Met-Ala-Gly-A and Z-Ala-Ala-Glu(OMe)-Ala-Ala-Leu-Met-Ala-Gly-A were obtained. It was shown that the condensation products can be split off from the support using the Met residue cleavage by BrCN.


Assuntos
Peptídeos/química , Dodecilsulfato de Sódio/química , Subtilisinas/química
3.
Biochemistry (Mosc) ; 64(10): 1122-7, 1999 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-10561558

RESUMO

The strain B-1166 differs from the other strains of Bacillus thuringiensis ssp. finitimus because it has two crystal types with different localization in the sporulating cell, i.e., inside and outside of exosporium membrane. Two dissociants of the strain were obtained containing only one of the crystal types. The initial strain produces at least three various delta-endotoxins (Fin2, Fin3, and Fin5) differing from all other known entomocidal proteins; Fin2 and Fin3 are similar to each other but differ from Fin5. Both crystal types contain the same endotoxins (Fin2, Fin3, and Fin5). In the B-1166 strain the site of crystal deposition is not determined by their protein composition.


Assuntos
Bacillus thuringiensis/química , Proteínas de Bactérias/química , Toxinas Bacterianas/química , Endotoxinas/química , Sequência de Aminoácidos , Bacillus thuringiensis/ultraestrutura , Toxinas de Bacillus thuringiensis , Cromatografia por Troca Iônica , Eletroforese em Gel de Poliacrilamida , Proteínas Hemolisinas , Imunodifusão , Microscopia Eletrônica
4.
Biochemistry (Mosc) ; 64(10): 1163-8, 1999 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-10561564

RESUMO

Proteins of molecular weight 65 and 62 kD and having affinity for toxins Cry4B and Cry11A produced by Bacillus thuringiensis ssp. israelensis have been isolated from brush border membranes of Aedes aegypti larvae using affinity chromatography. Using a ligand blotting technique, we show that the binding of these proteins to the biotinylated toxins is reversible and that the two toxins compete for binding to the two proteins. These proteins are likely to be Cry4B and Cry11A toxin receptors in gut epithelial cells of Aedes aegypti larvae.


Assuntos
Aedes/crescimento & desenvolvimento , Bacillus thuringiensis/metabolismo , Proteínas de Bactérias/metabolismo , Toxinas Bacterianas , Endotoxinas/metabolismo , Larva/metabolismo , Proteínas de Membrana/metabolismo , Animais , Toxinas de Bacillus thuringiensis , Ligação Competitiva , Cromatografia de Afinidade , Proteínas Hemolisinas , Proteínas de Membrana/isolamento & purificação , Ligação Proteica
5.
Biochemistry (Mosc) ; 64(9): 1030-7, 1999 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-10521720

RESUMO

A serine proteinase from roots of Taraxacum officinale Webb S. L. was isolated by affinity chromatography and gel-filtration on Superose 6R using FPLC. The enzyme is a 67-kD glycoprotein containing 54% carbohydrate which we have named taraxalisin. The substrate specificity of taraxalisin toward synthetic peptides and oxidized insulin B-chain is comparable with that of cucumisin from Cucumis melo and the subtilisin-like serine proteinase macluralisin from Maclura pomifera. The proteinase is inactivated by DFP and PMSF. Taraxalisin exhibits maximal activity at pH 8.0. The pH range for stability of the enzyme is narrow--6.0-9.0. The temperature optimum for the subtilisin-like activity is 40 degrees C. The N-terminal sequence of taraxalisin has 40% of its residues identical to those of subtilisin Carlsberg. Thus, the serine proteinase from dandelion roots is a member of the subtilisin family, which is evidently widespread in the plant kingdom.


Assuntos
Insulina/química , Insulina/metabolismo , Plantas/enzimologia , Serina Endopeptidases/química , Serina Endopeptidases/metabolismo , Sequência de Aminoácidos , Aminoácidos/análise , Animais , Bovinos , Cromatografia em Gel , Cinética , Dados de Sequência Molecular , Raízes de Plantas/enzimologia , Inibidores de Proteases/farmacologia , Serina Endopeptidases/isolamento & purificação , Especificidade por Substrato
6.
J Protein Chem ; 18(1): 21-7, 1999 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-10071925

RESUMO

The glutamyl endopeptidase gene of Bacillus intermedius was cloned from a genomic library expressed in Bacillus subtilis and sequenced (EMBL accession number Y15136). The encoded preproenzyme contains 303 amino acid residues; the mature 23-kDa enzyme consists of 215 residues. The mature enzyme reveals 38% of identical residues when aligned with the glutamyl endopeptidase from Bacillus licheniformis, whereas only five invariant residues were found among all known glutamyl endopeptidases. The amino acid residues that form the catalytic triad (H47, D98, and S171) as well as H186 participating in the binding of the substrate carboxyl group were identified. It seems that the structural elements responsible for the function of glutamyl endopeptidases from various sources are highly variable.


Assuntos
Bacillus/enzimologia , Bacillus/genética , Genes Bacterianos , Serina Endopeptidases/genética , Sequência de Aminoácidos , Bacillus subtilis/genética , Sequência de Bases , Clonagem Molecular , Biblioteca Gênica , Modelos Biológicos , Dados de Sequência Molecular , Filogenia , Proteínas Recombinantes , Análise de Sequência de DNA , Homologia de Sequência de Aminoácidos , Staphylococcus aureus/genética
7.
Bioorg Khim ; 25(9): 652-7, 1999 Sep.
Artigo em Russo | MEDLINE | ID: mdl-10624558

RESUMO

It was shown that acetylated dipeptides, Ac-D-Phe-D-Phe-OH, Ac-L-Phe-L-Phe-OH, Ac-D-Phe-L-Phe-OH, and Ac-L-Phe-D-Phe-OH, are formed during D-phenylalanine racemization. The overall content of these dipeptides in the reaction mixture ranged from 40 to 60% depending on the reaction conditions. We concluded that, like alpha-aminoisobutyric acid, phenylalanine is prone to polymerization under racemization conditions.


Assuntos
Fenilalanina/síntese química , Cromatografia Líquida de Alta Pressão , Espectrometria de Massas , Fenilalanina/química , Estereoisomerismo
8.
Bioorg Med Chem ; 7(12): 2953-9, 1999 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-10658601

RESUMO

Two ways for semi-enzymatic preparation of the peptide aldehydes are proposed: (1) enzymatic acylation of amino alcohols with acyl peptide esters and subsequent chemical oxidation of the resulting peptide alcohols with DMSO/acetic anhydride mixture or (2) enzymatic acylation of the preliminarily obtained by a chemical route amino aldehyde semicarbazones. Subtilisin 72, serine proteinase with a broad specificity, distributed over macroporous silica, was used as a catalyst in both cases. Due to the practical absence of water in the reaction mixtures the yields of the products in both enzymatic reactions were nearly quantitative. The second way seems to be more attractive because all chemical stages were carried out with amino acid derivatives, far less valuable compounds than peptide ones. A series of peptide aldehydes of general formula Z-Ala-Ala-Xaa-al (where Xaa-al = leucinal, phenylalaninal, alaninal, valinal) was obtained. The inhibition parameters for these compounds, in the hydrolysis reactions of corresponding chromogenic substrates for subtilisin and alpha-chymotrypsin, were determined.


Assuntos
Aldeídos/síntese química , Oligopeptídeos/síntese química , Acilação , Aldeídos/química , Aldeídos/farmacologia , Compostos Cromogênicos , Quimotripsina/antagonistas & inibidores , Inibidores Enzimáticos/síntese química , Inibidores Enzimáticos/química , Inibidores Enzimáticos/farmacologia , Cinética , Espectroscopia de Ressonância Magnética , Oligopeptídeos/química , Oligopeptídeos/farmacologia , Oxirredução , Relação Estrutura-Atividade , Subtilisinas/antagonistas & inibidores
9.
FEBS Lett ; 437(3): 237-40, 1998 Oct 23.
Artigo em Inglês | MEDLINE | ID: mdl-9824298

RESUMO

Latex of dandelion roots contains a serine proteinase that hydrolyzes a chromogenic peptide substrate Glp-Ala-Ala-Leu-pNA optimally at pH 8.0. Maximal activity of the proteinase in the roots is attained in April, at the beginning of plant development after the winter period. The protease was isolated by ammonium sulfate precipitation of the root extract followed by affinity chromatography on a Sepharose-Ala-Ala-Leu-mrp and gel filtration on Superose 6R performed in FPLC regime. Pure serine proteinase named taraxalisin was inactivated by specific inhibitors of serine proteinases, diisopropylfluorophosphate (DFP) and phenylmethylsulfonylfluoride (PMSF). Its molecular mass is 67 kDa and pI 4.5. pH stability range is 6-9 in the presence of 2 mM Ca2+, temperature optimum is at 40 degrees C; Km=0.37+/-0.06 mM. The substrate specificity of taraxalisin towards synthetic peptides and insulin B-chain is comparable with that of two other subtilisin-like serine proteinases, cucumisin and macluralisin. The taraxalisin N-terminal sequence traced for 15 residues revealed 40% coinciding residues when aligned with that of subtilisin Carlsberg.


Assuntos
Asteraceae/enzimologia , Proteínas de Plantas/isolamento & purificação , Serina Endopeptidases/isolamento & purificação , Sequência de Aminoácidos , Animais , Bovinos , Ativação Enzimática , Dados de Sequência Molecular , Peso Molecular , Proteínas de Plantas/química , Proteínas de Plantas/metabolismo , Raízes de Plantas , Homologia de Sequência de Aminoácidos , Serina Endopeptidases/química , Serina Endopeptidases/metabolismo , Especificidade por Substrato
10.
Biochem Mol Biol Int ; 45(6): 1265-71, 1998 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-9762424

RESUMO

A pair of highly degenerated primers was adapted to carry out a single-step PCR-detection of any known and probably unknown cry genes of classes cry1, cry4 and cry9 encoding for 130 kDa protein delta-endotoxins in the natural Bacillus thuringiensis (BT) strains. The Southern hybridization of the product has demonstrated that essentially remote cry-genes like cry1Aa and cry9A (cryIG) could be represented in the single amplificate if they are simultaneously present in the genome of the analyzed strain. Four genes were detected by the proposed scheme in the BT ssp. galleriae 11-67. One of them, gene cry1Ga1 was originally found and cloned using the PCR-amplification product obtained from the genomic DNA of this strain as a probe. The new gene was completely identical to one cloned by B. Lambert (unpublished, EMBL accession number Z22510) and essentially related to cryIM (EMBL accession number Y09326), renamed according to the new nomenclature as cry1Ga2.


Assuntos
Bacillus thuringiensis/genética , Genes Bacterianos , Genoma Bacteriano , Reação em Cadeia da Polimerase/métodos , Toxinas Bacterianas/genética , Sequência de Bases , Dados de Sequência Molecular , Alinhamento de Sequência
11.
Vopr Med Khim ; 44(3): 305-11, 1998.
Artigo em Russo | MEDLINE | ID: mdl-9703633

RESUMO

Protease activities in serum and urine of 116 children with glomerulonephritis and 16 healthy children were tested using chromogenic peptide substrates Z-Dala_Leu-Arg-pNA and Glp-Ala-ALa-Leu-pNa. We found the dependence between activity of serine proteinases and clinical, morphological forms of primary glomerulonephritis and hypertension.


Assuntos
Quimotripsina/metabolismo , Glomerulonefrite/enzimologia , Tripsina/metabolismo , Adolescente , Criança , Pré-Escolar , Quimotripsina/sangue , Quimotripsina/urina , Glomerulonefrite/sangue , Glomerulonefrite/complicações , Humanos , Hipertensão/complicações , Hipertensão/enzimologia , Especificidade por Substrato , Tripsina/sangue , Tripsina/urina
12.
J Protein Chem ; 17(5): 463-71, 1998 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-9717741

RESUMO

Bacillus thuringiensis "true" toxins consist of three domains: the N-terminal, alpha-helical domain followed by two beta-structural domains. Their limited proteolysis does not proceed at the domain boundaries, but is directed to the loops within the domains. There are at least two patterns of the limited proteolysis of "true" toxins. The first pattern, observed for CryIA and CryIVD delta-endotoxins, results in the proteolysis of the loops connecting beta-strands of the second domain. The second pattern, detected for CryIG and CryIVB proteins, consists in the cleavage of the loop connecting the fifth and the sixth alpha-helices of the first domain. The choice between the routes depends on the size, sequence, and dynamics of the loop that define its accessibility to a proteinase. Bioassay of CryIG and CryIVB delta-endotoxin fragments indicates that only two alpha-helices, the sixth and the seventh within the first domain, followed by the two beta-structural domains are sufficient for the insecticidal activity.


Assuntos
Toxinas Bacterianas , Endotoxinas/metabolismo , Aedes/embriologia , Sequência de Aminoácidos , Animais , Toxinas de Bacillus thuringiensis , Proteínas de Bactérias/metabolismo , Endotoxinas/química , Endotoxinas/isolamento & purificação , Proteínas Hemolisinas , Hidrólise , Larva , Manduca , Dados de Sequência Molecular , Controle Biológico de Vetores , Estrutura Terciária de Proteína , Homologia de Sequência de Aminoácidos
13.
Bioorg Khim ; 24(3): 175-8, 1998 Mar.
Artigo em Russo | MEDLINE | ID: mdl-9612558

RESUMO

Chromogenic hexapeptides Dnp-Ala-Ala/Ser-Phe-Phe-Ala-Arg-NH2 containing a Phe-Phe bond, which is sensitive to aspartic proteinases, were used as substrates for assaying the activity of pepsin, chymosin, and aspergillopepsin A. The assay was performed after the separation of hydrolyzates on SP-Sephadex by measuring at 360 nm the absorbance of the dinitrophenylpeptide lacking the cationic group, which was formed upon the cleavage of the substrate. The kinetic parameters of the hydrolysis of the substrates were evaluated. It is shown that replacing the Ala residue with Ser in the P2 position does not substantially change the kinetic parameters. The substrates were hydrolyzed by pepsin several times faster than by aspergillopepsin A or chymosin. The method is sensitive and enables the activity of aspartic proteinases to be determined easily.


Assuntos
Ácido Aspártico Endopeptidases/química , Compostos Cromogênicos/química , Oligopeptídeos/química , Alanina/química , Quimosina/química , Dinitrofenóis/química , Concentração de Íons de Hidrogênio , Hidrólise , Cinética , Pepsina A/química , Serina/química , Espectrofotometria Ultravioleta , Especificidade por Substrato
14.
Bioorg Khim ; 24(4): 306-12, 1998 Apr.
Artigo em Russo | MEDLINE | ID: mdl-9612574

RESUMO

The behavior of subtilisin 72 in some aprotic solvents (acetonitrile, dioxane, and tetrahydrofurane) was studied. The enzyme was shown to be partially soluble in tetrahydrofurane, but it is rendered profoundly inactive in this solution. In acetonitrile and dioxane, subtilisin formed dilute suspensions whose activities were measured after dilution with water. Under these conditions, subtilisin suspended in acetonitrile manifested an activity that was an order of magnitude higher than that of its dioxane suspension, and this activity continued for a long time. Z-Ala-Ala-Leu-pNA was synthesized from Z-Ala-Ala-OCH3 and Leu-pNA under the catalysis by dilute suspension of subtilisin in acetonitrile. p-Nitroanilides of tetrapeptides, Z-Ala-Ala-P1-P'1-pNA, where P1 and P'1 were either Leu or Phe, were similarly synthesized in acetonitrile under catalysis by dilute subtilisin suspension at [S]:[E] = 10(5):1. p-Nitroanilides of tripeptides, Z-Ala-Ala-Leu-pNA, Z-Ala-Ala-Phe-pNA, and Z-Ala-Ala-Phe-NH2, were also synthesized in the presence of a concentrated subtilisin suspension at [S]:[E] = 10(3):1. It was shown that the increase in enzyme concentration resulted in the double coupling of nucleophile, and Z-Ala-Ala-Leu-Leu-pNA, Z-Ala-Ala-Phe-Phe-pNA, and Z-Ala-Ala-Phe-Phe-NH2 were obtained with 13, 33, and 40% yields, respectively. Therefore, such reaction systems can be used for creating long hydrophobic peptides whose synthesis in water-organic mixtures is difficult due to the poor solubility of starting components in aqueous buffer solutions.


Assuntos
Oligopeptídeos/síntese química , Solventes/química , Subtilisinas/química , Acetonitrilas/química , Soluções Tampão , Catálise , Cromatografia Líquida de Alta Pressão , Dioxanos/química , Furanos/química , Solubilidade , Espectrofotometria Ultravioleta , Suspensões
15.
Bioorg Khim ; 24(1): 10-5, 1998 Jan.
Artigo em Russo | MEDLINE | ID: mdl-9551195

RESUMO

A general method was developed for the synthesis of new chromogenic substrates of aspartyl proteases: Dnp-Ala-Xaa-Phe-Phe-Ala-Arg-NH2, where Xaa was Ala or Ser. The synthetic scheme involved both chemical and enzymic stages, the condensation of tripeptides in an organic medium by means of pepsin immobilized on Celite being among the latters. The influence of organic solvents, reaction time, and the composition and ionic strength of the buffers used in the reaction mixture and at the pepsin immobilization step on the efficacy of the pepsin-catalyzed synthesis was studied.


Assuntos
Ácido Aspártico Endopeptidases/química , Compostos Cromogênicos/síntese química , Alanina/química , Soluções Tampão , Catálise , Terra de Diatomáceas/química , Enzimas Imobilizadas , Concentração Osmolar , Pepsina A/química , Serina/química , Solventes/química , Especificidade por Substrato
16.
FEMS Microbiol Lett ; 159(2): 145-50, 1998 Feb 15.
Artigo em Inglês | MEDLINE | ID: mdl-9503606

RESUMO

The structural gene of the carboxypeptidase T (cpt) was successfully expressed in cell wall-less L-form cells of Proteus mirabilis. The DNA sequence encoding the PhoA leader peptide was fused with a truncated cpt gene encoding the mature enzyme. The modified gene in a pUC-based kanamycin resistance vector under the control of the lac promoter was transformed into L-form cells of P. mirabilis. They were able to produce the recombinant CpT both as a secretory and as a cell-bound insoluble form. The co-secretory processing of the PhoA leader peptide was quite efficient. The yield of the secreted CpT was not less than 20 mg l-1 and should be improvable.


Assuntos
Proteínas de Bactérias , Carboxipeptidases/genética , Formas L/genética , Micromonosporaceae/genética , Proteus mirabilis/genética , Sequência de Aminoácidos , Sequência de Bases , Dados de Sequência Molecular , Proteínas Recombinantes/metabolismo
17.
Biochemistry (Mosc) ; 63(12): 1419-23, 1998 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-9916160

RESUMO

P33 protein was isolated from the cell walls of Candida utilis. Homology between P33 and Bgl2p proteins from the cell walls of Saccharomyces cerevisiae was shown. The important role of these proteins in molecular organization of yeast cell walls was demonstrated using trypsin proteolysis and the "gene disruption" method.


Assuntos
Candida/genética , Parede Celular/metabolismo , Proteínas Fúngicas/genética , Glucana Endo-1,3-beta-D-Glucosidase/genética , Proteínas de Saccharomyces cerevisiae , Saccharomyces cerevisiae/genética , Candida/metabolismo , Clonagem Molecular , Humanos , Recém-Nascido , Saccharomyces cerevisiae/metabolismo , Homologia de Sequência
18.
Bioorg Khim ; 24(2): 112-8, 1998 Feb.
Artigo em Russo | MEDLINE | ID: mdl-10335406

RESUMO

Trypsin PC from the hepatopancreas of the king crab Paralithodes camtschatica was isolated and purified to apparent homogeneity by ion-exchange chromatography on Aminosilochrom and DEAE-Sephadex and affinity chromatography on arginine-agarose. The yield of the enzyme was 37.7%, and the purification degree was 21. Trypsin PC has a molecular mass of 29 kDa and pI < 2.5. It hydrolysis N-benzoyl-L-arginine p-nitroanilide at the optimum pH of 7.5-8.0 and at the temperature optimum of 55 degrees C (K(m) = 0.05 mM). Trypsin PC retained its activity within the pH range of 5.8-9.0 in the presence of Ca2+. The enzyme was inhibited by the specific inhibitors of serine proteases diisopropyl fluorophoshate and phenylmethylsulfonyl fluoride, by the trypsin inhibitor N-tosyl-L-lysylchloromethylketone, and by the trypsin inhibitors from soybean and potato. Trypsin PC was found to hydrolyze amide bonds formed by carboxylic groups of lysine and arginine in peptide substrates. The N-terminal sequence of this enzyme is IVGGTEVTPG.


Assuntos
Braquiúros/enzimologia , Tripsina/isolamento & purificação , Sequência de Aminoácidos , Animais , Bovinos , Cromatografia de Afinidade , Cromatografia por Troca Iônica , Colágeno/metabolismo , Eletroforese em Gel de Poliacrilamida , Estabilidade Enzimática , Fibrinogênio/metabolismo , Concentração de Íons de Hidrogênio , Ponto Isoelétrico , Fígado/enzimologia , Peso Molecular , Pâncreas/enzimologia , Homologia de Sequência de Aminoácidos , Especificidade por Substrato , Tripsina/química , Tripsina/metabolismo , Inibidores da Tripsina/farmacologia
19.
Biochemistry (Mosc) ; 62(8): 903-8, 1997 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-9360302

RESUMO

A homogeneous glutamyl endopeptidase splitting peptide bonds of glutamic and, rarely, of aspartic acid residues in peptides and proteins was isolated from Bacillus intermedius 3-19 culture filtrate using chromatography on CM-cellulose and Mono S. The enzyme molecular mass is 29 kD and the pI is 8.4. The proteinase is inhibited by DFP. The enzyme, like other glutamyl endopeptidases, reveals two pH optima (pH 7.5 and 9.0) for casein and one (pH 8.0) for Z-Glu-pNA hydrolysis. The K(m) for the hydrolysis of the latter substrate is 6 mM. The enzyme activity is optimal at 55 degrees C. The enzyme is stable in the pH range 6.5-11.0. Its N-terminal sequence shows 56% coinciding residues when compared with that of Bacillus licheniformis glutamyl endopeptidase. Crystal prisms or plates 0.25-0.3 x 0.15 x 0.07-0.1 mm have been grown using the vapor diffusion technique in a hanging drop followed by macroseeding. The crystals belong to the space group B2 with the following unit cell parameters: a = 69.59 A; b = 61.61 A; c = 56.11 A; gamma = 117.57 degrees. The X-ray data set to 1.7 A resolution has been collected on an automatic synchrotron (EMBL Hamburg Station).


Assuntos
Bacillus/enzimologia , Serina Endopeptidases/isolamento & purificação , Sequência de Aminoácidos , Cristalização , Concentração de Íons de Hidrogênio , Hidrólise , Dados de Sequência Molecular , Inibidores de Proteases/farmacologia , Serina Endopeptidases/química , Serina Endopeptidases/metabolismo , Especificidade por Substrato
20.
Med Parazitol (Mosk) ; (2): 44-7, 1997.
Artigo em Russo | MEDLINE | ID: mdl-9304034

RESUMO

Examining zoonotic infections in the plague foci in Kazakhstan over a decade has revealed their wide spread of vectors of pseudotuberculosis, intestinal Yersinia infection, pasteurellosis, listeriosis, salmonellosis, erysipeloid. Some causative agents under study can regulate the number of the main vector in the foci of plague, hamper the bacteriological and serological diagnosis of plague and be of predictive value in the assessment of the epizootic situation.


Assuntos
Reservatórios de Doenças/veterinária , Peste/epidemiologia , Zoonoses/epidemiologia , Animais , Animais Selvagens , Portador Sadio/epidemiologia , Portador Sadio/imunologia , Portador Sadio/veterinária , Vetores de Doenças , Cazaquistão/epidemiologia , Peste/veterinária , Estudos Soroepidemiológicos
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