Base de dados : LILACS
Pesquisa : D08.811.913.400.450.400 [Categoria DeCS]
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Id: lil-633699
Autor: De La Vega Elena, Carlos D.; Hellberg, Åsa; Bonetti, Sofía; Gonzalez, Carlos A.; Chialina, Sergio; Raillon, Miguel A.; Pivetta, Mario A.; Solis, Edita A.; Olsson, Martin L..
Título: Un caso de grupo sanguíneo raro: fenotipo p / A rare blood group: p phenotype
Fonte: Medicina (B.Aires);69(6):651-654, nov.-dic. 2009. ilus.
Idioma: es.
Resumo: Un individuo con un fenotipo eritrocitario raro carece de uno o varios antígenos presentes en la mayor parte de la población de pertenencia. Cuando presenta el anticuerpo correspondiente, se pueden producir complicaciones perinatales, transfusionales y/o transplantológicas. Se presenta el caso de una embarazada aloinmunizada derivada a nuestro servicio en la semana 12 de su tercera gesta para su evaluación y seguimiento. El diagnóstico inmunohematológico le asignó el excepcional fenotipo "p" (aproximadamente 1/200 000 individuos), asociado con una mayor tasa de abortos espontáneos y a reacciones transfusionales graves cuando se transfunden unidades incompatibles. El estudio del gen A4GALT demostró la presencia de la mutación c.752C > T en doble dosis. Esta mutación lleva a un cambio de una prolina por una leucina en el residuo 251 de la 4-α-galactosiltransferasa. Por parto inducido por sufrimiento fetal, nace a las 36 semanas una bebé con prueba de antiglobulina (Coombs) directa negativa, eluido reactivo, con ictericia que requirió luminoterapia. Una semana después el neonato fue externado sin secuelas aparentes. Posteriormente, a raíz de una cirugía inminente y la improbabilidad de encontrar sangre compatible, se elaboró un plan para cubrir las posibles demandas. Este caso pone en evidencia la necesidad de contar a nivel nacional con un laboratorio de referencia de inmunohematología y un banco de sangre de grupos raros, que permita resolver con celeridad situaciones que requieran transfundir a estos individuos.

A rare blood group is usually defined as the absence of a high prevalence antigen or the absence of several antigens within a single blood group system. These individuals may develop clinically significant red cell antibodies to the high incidence red cell antigens they lack. A 33-year-old alloimmunized woman was referred to our center at the 12th week of her third pregnancy for evaluation and follow up. The laboratory work-up grouped her as belonging to "p" phenotype, associated with difficulties to find compatible blood for transfusion and a high incidence of recurrent miscarriage. At 36 weeks, a baby girl was born by induced labor due to fetal suffering. With a negative direct antiglobulin test but a positive elution test, she was in the neonatology ward for one week receiving luminotherapy. Homozygosity for a missense mutation at position 752 (c.752C > T) in the A4GALT gene was found to be responsible for the p phenotype. This mutation changes a proline to a leucine at codon 251 of the 4-α-galactosyltransferase. Recently, due to an imminent chirurgical intervention and the impossibility to have compatible blood available for transfusion, an autologous donation plan was designed to satisfy probable demand. This case showed the need for blood bank facilities capable to respond satisfactorily to these situations in Argentina. This would facilitate the storage of cryopreserved blood from individuals with rare blood groups for homologous use or to develop rare blood donors programs.
Descritores: Eritroblastose Fetal/sangue
Galactosiltransferases/genética
Mutação de Sentido Incorreto
Sistema do Grupo Sanguíneo P/genética
Fenótipo
-Sequência de Bases
Transfusão de Sangue
Glicosiltransferases/análise
Limites: Adulto
Feminino
Humanos
Gravidez
Tipo de Publ: Relatos de Casos
Responsável: AR1.2 - Instituto de Investigaciónes Epidemiológicas


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Texto completo SciELO Brasil
Texto completo
Id: lil-253783
Autor: Cruz, Rubens; Cruz, Vinícius D'Arcádia; Belote, Juliana Gisele; Khenayfes, Marcelo de Oliveira; Dorta, Claudia; Oliveira, Luiza Helena dos Santos.
Título: Properties of a new fungal ß-Galactosidase with potential application in the dairy industry
Fonte: Rev. microbiol;30(3):265-71, jul.-set. 1999. tab, graf.
Idioma: pt; en.
Resumo: ß-Galactosidase or ß-D-galactohydrolase (EC.3.2.1.23) is an important enzyme industrially used for the hydrolysis of lactose from milk and milk whey for several applications. Lately, the importance of this enzyme was enhanced by its galactosyltransferase activity, which is responsible for the synthesis of transgalctosylated oligosaccharides (TOS) that act as functional foods, with several beneficial effects on consumers. Penicillium simplicissimum, a strain isolated from soil, when grown in semi-solid medium showed good productivity of ß-galactosidase with galactosyltransferase activity. The optimum pH for hydrolysis was in 4.0-4.6 range and the optimum pH for galactosyltransferase activity was in the 6.0-7.0 range. The optimum temperature for hydrolysis and transferase activity was 55-60§C and 50§C, respectively, and the enzyme showed high thermostability for the hydrolytic activity. The enzyme showed a potential for several industrial applications such as removal of 67 (per cent) of the lactose from milk and 84 (per cent) of the lactose from milk whey when incubated at their original pH (4.5 and 6.34, respectively) under optimum temperature conditions. When incubated with a 40 (per cent) lactose solution in 150 mM McIlvaine buffer, pH 4.5, at 55§C the enzyme converted 86.5 (per cent) of the lactose to its component monosaccharides. When incubated with a 60 (per cent) lactose solution in the same buffer but at pH 6.5 and 50§C, the enzyme can synthetize up to 30.5 (per cent) TOS, with 39.5 (per cent) lactose and 30 (per cent) monosaccharides remaining in the preparation.
Descritores: beta-Galactosidase/metabolismo
Fungicidas Industriais/metabolismo
-beta-Galactosidase/química
Fungicidas Industriais/química
Galactosiltransferases/metabolismo
Responsável: BR32.1 - Serviço de Biblioteca e Informação Biomédica


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Almeida, Igor C
Takahashi, Helio K
Id: lil-196740
Autor: Travassos, Luiz R; Almeida, Igor C; Takahashi, Helio K.
Título: Carbohydrate epitopes: structure and presentation and the reactivity of biological ligands: recognition of alpha-D-Galp NAc and alpha-D-Galp conformational structures
Fonte: Ciênc. cult. (Säo Paulo);46(4):242-8, July-Aug. 1994.
Idioma: en.
Resumo: Apart from glycolipids and glycoproteins that express A and B blood group antigens which contain terminal nonreducing units of alpha-D-Galp NAc and alpha-D-Galp respectively, there are several other glycoconjugates in nature that contain these units linked to unfucosylated saccharides or protein. They represent normal products of the action of specific glycosyl-transferases in primate and nonprimate mammalian cells, protozoa and a few other microorganisms, end-units of carbohydrate components that have not benn further processed by additional glycosylation, or neo-antigens resulting from deregulation of certain transferases as in tumor cells. Biological ligands recognizing these structures include mono and polyclonal antibodies, bacterial fimbriae and laminin. Binding depends on the linkages and sequence of the carbohydrate chain, but also on the epitope conformation as influenced by adjacent substitution, angling determined by the glycoconjugate-substrate interaction, steric hindrance and other factors. These aspects are discussed in this minireview.
Descritores: Carboidratos/química
Epitopos/química
Glicoconjugados/química
-Carboidratos/imunologia
Proteínas de Transporte
Dissacarídeos
Epitopos/imunologia
Galactosiltransferases
Glicoconjugados/imunologia
Glicosiltransferases
Limites: Humanos
Animais
Tipo de Publ: Revisão
Responsável: BR1.1 - BIREME


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Fotocópia
Id: lil-138276
Autor: Turco, S; Descoteaux, A; Ryan, K; Garraway, L; Beverley, S.
Título: Isolation of virulence genes directing GPI synthesis by functional complementation of Leishmania
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;27(2):133-8, Feb. 1994. ilus.
Idioma: en.
Conferência: Apresentado em: GPI-Anchor Proteins: Structure and Function - 1994 Meeting, Angra dos Reis, 20-26 Feb. 1994.
Resumo: Recent advances in molecular genetics of Leishmania parasites prompted us to develop methods of functional genetic complementation in Leishmania and apply them to the isolation of genes involved in the biosynthesis of the virulence determinant LPG, an abundant GPI-anchored polysaccharide. LPG1, the gene product identified by complementation of our R2D2 LPG- mutant, may be a glycosyltransferase responsible for the addition of galactofuranose to the nascent chain. As galactofuranose is not found in mammalian cells, inhibition of the addition of this sugar could be exploited for chemotherapy. Overall, the success of the functional complementation approach opens the way to the identification of a variety of genes involved in pathogenesis and parasitism
Descritores: Fosfatidilinositóis/biossíntese
Teste de Complementação Genética
Glicolipídeos/biossíntese
Leishmania donovani/genética
Leishmania/genética
Virulência/genética
-Aglutinação
Sequência de Aminoácidos
Anticorpos Monoclonais
Sequência de Bases
Cosmídeos
DNA de Protozoário/genética
DNA de Protozoário/metabolismo
Galactosiltransferases/biossíntese
Biblioteca Gênica
Leishmania donovani/patogenicidade
Leishmania/patogenicidade
Dados de Sequência Molecular
Limites: Animais
Responsável: BR26.1 - Biblioteca Central


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Zancan, G. T
Id: lil-63326
Autor: Kubicki, D; Zancan, G. T; Amaral, D.
Título: A Dactylium dendroides morphological mutant defective in D-galactose metabolism
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;21(5):895-902, 1988. ilus, tab.
Idioma: en.
Projeto: CNPq.
Resumo: 1. A morphological mutant of the mold Dactylium dendroides was and the phenotype characterized as D-Gal-and L-Ara-. 2. The transport system for D-galactose seemed to be inducible in wild type and mutant and was altered in the mutant. 3. Galactose-1-P- uridylyl transferase activity was absent in the mutant. 4. The levels of intracellular galactose oxidase activity were similar in the wild type and in the mutant, theraby excluding a possible participation of this enzymes in glactose catabolism inthe mold. 5. The low level of galactose oxidase activity found in the extracellular medium indicates a defect in galactose oxidase secretion by the mutant
Descritores: Galactose Oxidase/metabolismo
Galactosiltransferases/metabolismo
Fungos Mitospóricos
Mutação
UTP-Hexose-1-Fosfato Uridililtransferase/metabolismo
Responsável: BR26.1 - Biblioteca Central



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