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1.
Chem Biodivers ; 11(8): 1140-50, 2014 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-25146760

RESUMO

In this work, we investigated whether materials isolated from algae that threaten ecosystems can be used for human benefit. We converted acidic polysaccharides (ulvan) from the alga Ulva pertusa into soft hydrogel materials. In addition to ulvan, the hydrogels also contained alginate in a polyion complex with chitosan. Cross-linking the hydrogel with glutaraldehyde reduced polysaccharide elution from the polyion complex gel. We also found that both ulvan-chitosan and alginate-chitosan gels were able to remove urea and heavy metals from aqueous solution. This is clinically significant, since during apheresis, toxic compounds such as urea have to be removed from the bloodstream of patients. Importantly, albumin was not removed by the hydrogels, implying that this vital protein can be returned to the bloodstream following dialysis.


Assuntos
Remoção de Componentes Sanguíneos , Hidrogéis , Polissacarídeos/química , Ulva/química , Adsorção , Albuminas/química , Alginatos , Quitosana , Ácido Glucurônico , Ácidos Hexurônicos , Metais Pesados/química , Peso Molecular , Espectroscopia de Infravermelho com Transformada de Fourier , Ureia/isolamento & purificação
2.
Protein Pept Lett ; 12(2): 207-10, 2005 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-15723648

RESUMO

We developed a simple immobilisation method for His-tagged enzymes on a microchannel surface. It facilitates immobilisation of protein molecule on microchannel surface through Ni-complex, using crude or purified protein solutions. By this method, we could immobilize proteins on microcapillary constantly. This method might be useful for further development of microreactor with reversibly immobilized enzymes.


Assuntos
Reatores Biológicos , Enzimas Imobilizadas/química , Histidina/química , Animais , Enzimas Imobilizadas/metabolismo , L-Lactato Desidrogenase/química , L-Lactato Desidrogenase/metabolismo , Estrutura Molecular , Propriedades de Superfície
3.
Lab Chip ; 2(1): 15-8, 2002 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-15100854

RESUMO

Glycosidase-promoted hydrolysis was performed in a microreaction channel. The result was compared with the reaction in a micro-test tube. Transgalactosylation on p-nitrophenyl-2-acetamide-2-deoxy-beta-D-glucopyranoside was also examined in a microreaction channel, because transglycosylation is a useful method for oligosaccharide synthesis. We examined both the forward reaction, i.e., hydrolysis, and the reverse reaction, i.e., transglycosylation, in the microreaction channel. The results showed that both hydrolysis and transglycosylation were enhanced in the microreaction channel compared with the batch reaction.


Assuntos
Acetilglucosamina/análogos & derivados , Miniaturização , Oligossacarídeos/síntese química , beta-Galactosidase/química , Acetilglucosamina/química , Glicosilação
4.
Bioorg Med Chem Lett ; 15(1): 167-70, 2005 Jan 03.
Artigo em Inglês | MEDLINE | ID: mdl-15582433

RESUMO

Conjugate DNAzymes with polyamines and peptides were successfully prepared by solid phase fragment condensation (SPFC) and showed up to 4.2 times higher catalytic efficiency (k(cat)/K(m)) and enhanced tolerance against DNase 1digestion. To be pointed out, intracellular localization of DNAzymes could be controlled by conjugated with naturally occurring signal peptides responsible for nuclear cytoplasmic transport of proteins.


Assuntos
DNA Catalítico/metabolismo , RNA Viral/metabolismo , Sequência de Bases , Produtos do Gene gag/genética , HIV-1/genética , Hidrólise , RNA Viral/química
5.
Nucleic Acids Symp Ser (Oxf) ; (48): 99-100, 2004.
Artigo em Inglês | MEDLINE | ID: mdl-17150497

RESUMO

Precisely controlled intracellular delivery of oligonucleotides was achieved by conjugation with signal peptides and amphiphilic designed peptides. Localization in the cellular nucleus was accelerated by nuclear localizing signals derived from naturally occurring viral proteins and arginine rich designed peptides, and cytoplasmic localization was enhanced by nuclear export signals and membrane fusion peptides.


Assuntos
DNA/metabolismo , Sistemas de Liberação de Medicamentos , Peptídeos/metabolismo , Sequência de Aminoácidos , Morte Celular/efeitos dos fármacos , DNA/síntese química , Desoxirribonucleases/metabolismo , Humanos , Células Jurkat , Dados de Sequência Molecular , Oligonucleotídeos Antissenso/farmacologia , Peptídeos/síntese química , Peptídeos/química , Ribonuclease H/metabolismo , Telomerase/metabolismo
6.
Nucleic Acids Symp Ser (Oxf) ; (48): 303-4, 2004.
Artigo em Inglês | MEDLINE | ID: mdl-17150599

RESUMO

In the present study, membrane permeability and intracellular localization of oligonucleotide (ODN) conjugated with naturally occurring functional peptides or designed peptide were investigated, as well as antisense properties of them to inhibit of telomerase activities. All conjugate antisense ODNs showed higher membrane permeability and nuclease resistance than natural ODN. Intracellular localization of ODN could be precisely controlled by conjugation with functional peptides. Conjugate antisense ODNs indicated thousand fold higher inhibitory effects than natural ODN in cellular extract and 95% suppression in human leukemia cells.


Assuntos
Expressão Gênica , Técnicas de Transferência de Genes , Oligonucleotídeos Antissenso/metabolismo , Sinais Direcionadores de Proteínas , Sequência de Bases , Extratos Celulares , Sobrevivência Celular/efeitos dos fármacos , Expressão Gênica/efeitos dos fármacos , Humanos , Células Jurkat , Dados de Sequência Molecular , Oligonucleotídeos Antissenso/genética , Oligonucleotídeos Antissenso/farmacologia , Telomerase/antagonistas & inibidores
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