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Registros recuperados: 6
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Imprime registro no formato completo
2-Phenitidine derivatives as suitable inhibitors of butyrylcholinesterase BJPS
Abbasi,Muhammad Athar; Aziz-ur-Rehman,; Qureshi,Muhammad Zahid; Khan,Farhan Mehmood; Khan,Khalid Mohmmed; Ashraf,Muhammad; Afzal,Iftikhar.
This manuscript reports the synthesis of a series of N-substituted derivatives of 2-phenitidine. First, the reaction of 2-phenitidine (1) with benzene sulfonyl chloride (2) yielded N-(2-ethoxyphenyl) benzenesulfonamide (3), which further on treatment with sodium hydride and alkyl halides (4a-g) furnished into new sulfonamides (5a-g). Second, the phenitidine reacted with benzoyl chloride (6) and acetyl chloride (8) to yield the reported N-benzoyl phenitidine (7) and N-acetyl phenitidine (9), respectively. These derivatives were characterized by infrared spectroscopy, ¹H-NMR, and EI-MS, and then screened against acetylcholinesterase, butylcholinesterase, and lipoxygenase enzyme, and were found to be potent inhibitors of butyrylcholinesterase alone.
Tipo: Info:eu-repo/semantics/article Palavras-chave: 2-Phenitidine/inhibitor activity; Sulfonamides; Acetamide; Benzamide; Butyrylcholinesterase.
Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1984-82502013000100014
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Biochemical and genetic analysis of butyrylcholinesterase (BChE) in a family, due to prolonged neuromuscular blockade after the use of succinylcholine Genet. Mol. Biol.
Garcia,Daniel Fantozzi; Oliveira,Ticiano G.; Molfetta,Greice A.; Garcia,Luiz V.; Ferreira,Cristiane A.; Marques,Adriana A.; Silva Jr.,Wilson Araujo.
Butyrylcholinesterase (BChE) is a plasma enzyme that catalyzes the hydrolysis of choline esters, including the muscle-relaxant succinylcholine and mivacurium. Patients who present sustained neuromuscular blockade after using succinylcholine usually carry BChE variants with reduced enzyme activity or an acquired BChE deficiency. We report here the molecular basis of the BCHE gene underlying the slow catabolism of succinylcholine in a patient who underwent endoscopic nasal surgery. We measured the enzyme activity of BChE and extracted genomic DNA in order to study the promoter region and all exons of the BCHE gene of the patient, her parents and siblings. PCR products were sequenced and compared with reference sequences from GenBank. We detected that the...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Hereditary hypocholinesterasemia; Butyrylcholinesterase; Succinylcholine BCHE gene; DNA polymorphism.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572011000100008
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Molecular forms of butyrylcholinesterase and obesity Genet. Mol. Biol.
Boberg,Dellyana R.; Furtado-Alle,Lupe; Souza,Ricardo L.R.; Chautard-Freire-Maia,Eleidi A..
This study compared obese (N = 134) and unobese (N = 92) male blood donors, regarding the relative intensity (RI) and activity of different molecular forms (G1, G2, G4 and G1-ALB) of butyrylcholinesterase (BChE, EC 3.1.1.8) found in plasma, thereby searching for an association between these variables with obesity and SNPs of exons 1 and 4 of the BCHE gene. It was shown that obese and unobese individuals do not differ in the RI of each BChE band, even when classifying the sample into three genotypes of exons 1 and 4 of the BCHE gene (-116GG/539AA, -116GG/539AT, -116GA/539AT). Although the mean BChE activity of each band was significantly higher in obese than in unobese blood donors, the proportions of BChE bands were maintained, even under the metabolic...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Butyrylcholinesterase; Body mass index; Obesity; BCHE gene SNPs.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572010000300011
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Obesity and variants of the GHRL (ghrelin) and BCHE (butyrylcholinesterase) genes Genet. Mol. Biol.
Dantas,Vitor G.L.; Furtado-Alle,Lupe; Souza,Ricardo L.R.; Chautard-Freire-Maia,Eleidi A..
Ghrelin coded by the GHRL gene is related to weight-gain, its deactivation possibly depending on its hydrolyzation by butyrylcholinesterase (BChE) encoded by the BCHE gene, an enzyme already associated with the body mass index (BMI). The aim was to search for relationships between SNPs of the GHRL and BCHE genes with BChE activity, BMI and obesity in 144 obese and 153 nonobese Euro-Brazilian male blood donors. In the obese individuals, a significant association with higher BChE activity, in the 72LM+72MM; -116GG genotype class (GHRL and BCHE genes, respectively) was noted. No significant differences were found otherwise, through comparisons between obese and control individuals, of genotype and allele frequencies in SNPs of the GHRL gene (Arg51Gln and...
Tipo: Info:eu-repo/semantics/article Palavras-chave: BCHE gene; Body-mass index; Butyrylcholinesterase; Ghrelin; GHRL gene; Obesity.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572011000200006
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The powerful high pressure tool for protein conformational studies BJMBR
Marchal,S.; Torrent,J.; Masson,P.; Kornblatt,J.M.; Tortora,P.; Fusi,P.; Lange,R.; Balny,C..
The pressure behavior of proteins may be summarized as a the pressure-induced disordering of their structures. This thermodynamic parameter has effects on proteins that are similar but not identical to those induced by temperature, the other thermodynamic parameter. Of particular importance are the intermolecular interactions that follow partial protein unfolding and that give rise to the formation of fibrils. Because some proteins do not form fibrils under pressure, these observations can be related to the shape of the stability diagram. Weak interactions which are differently affected by hydrostatic pressure or temperature play a determinant role in protein stability. Pressure acts on the 2º, 3º and 4º structures of proteins which are maintained by...
Tipo: Info:eu-repo/semantics/article Palavras-chave: High pressure; Prion protein; Amyloid; Ataxin; Enolase; Butyrylcholinesterase.
Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800004
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Thermostabilisation of human serum butyrylcholinesterase for detection of its inhibitors in water and biological fluids BABT
Jaganathan,Lakshmanan; Boopathy,Rathanam.
The ability of gelatine-trehalose to convert the normally fragile, dry human serum BChE into a thermostable enzyme and its use in the detection of cholinesterase inhibitors in water and biological fluids is described. Gelatine or trehalose alone is unable to protect the dry enzyme against exposure to high temperature, while a combination of gelatine and trehalose were able to protect the enzyme activity against prolonged exposure to temperature as high as +50°C. A method for rapid, simple and inexpensive means of screening for cholinesterase inhibitors such as carbamates and organophosphates in water, vegetables and human blood has been developed.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Butyrylcholinesterase; Carbamates; Cholinesterase; Gelatine; Organophosphorus; Trehalose.
Ano: 1999 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89131999000300012
Registros recuperados: 6
Primeira ... 1 ... Última
 

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