Reductive Alkylation
Mostrando 1-9 de 9 artigos, teses e dissertações.
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1. Alquilação redutiva da quitosana a partir do glutaraldeído e 3-amino-1-pr / Reductive alkylation of chitosan by glutaraldehyde and 3-amino-1-propanol
Chitosan derivatives were prepared by reductive alkylation using glutaraldehyde and 3-amino-1-propanol. The reducing agent used was the sodium borohydride. Tests of solubility, stability and viscosity were performed in order to evaluate these parameters effects in the reaction conditions (molar ratio of the reactants and presence of nitrogen in the reaction
Publicado em: 2008
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2. Sintese total e enantiosseletiva da aglicona do antibiotico (+)-10-desoximetimicina
This work describes the enantioselective total synthesis of (+)-10-Deoxymethynolide (2c), the aglycon of the 12-membered macrolide antibiotic 10-Deoxymethymycin, through the esterification of the C1-C7 and C8-C13 fragments ((-)-339 and (+)-346, respectively) and macrocyclization of the corresponding vinylic iodide-aldehyde via an intramolecular Nozaki- Hiyam
Publicado em: 1998
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3. Radioisotopic labeling of human papovavirus (BK) by iodination and reductive alkylation.
Purified virions of the GS strain of the BK group of human papovaviruses were labeled with 125I using chloramine T or lactoperoxidase or with tritium using sodium borohydride. All viral polypeptides were labeled. Tryptic digests of iodinated VP1 were analyzed.
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4. Properties of Feline Leukemia Virus II. In Vitro Labeling of the Polypeptides 1
Radioactive labeling of proteins from guanidine-hydrochloride disrupted feline leukemia virus was done in vitro by attaching [3H]methyl groups to protein amino groups with reductive alkylation. When in vitro labeled disrupted virus was analyzed by gel filtration in the presence of 6 M guanidine-hydrochloride the expected six major and one minor protein peaks
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5. Production and characterization of aflatoxin B2a antiserum.
The specificity and sensitivity of antiserum elicited from rabbits against aflatoxin B2a-bovine serum albumin conjugates were characterized with a radioimmunoassay (RIA) and an enzyme-linked immunosorbent assay (ELISA). Aflatoxin B1 was first converted to aflatoxin B2a and then conjugated to bovine serum albumin and horseradish peroxidase by a reductive alky
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6. The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose.
Cellulose-binding domains (CBDs) bind specifically to cellulose, and form distinct domains of most cellulose degrading enzymes. The CBD-mediated binding of the enzyme has a fundamental role in the hydrolysis of the solid cellulose substrate. In this work we have investigated the reversibility and kinetics of the binding of the CBD from Trichoderma reesei cel
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7. Purification and characterization of initiation factor IF-E3 from rabbit reticulocytes.
Initiation factor IF-E3 from rabbit reticulocytes was isolated from a high salf extract of ribosomes prepared according to the procedure of Schreier and Staehelin (J. Mol9 Biol, 73, 329-349, 1973). The factor was highly purified from the crude extract by ammonium sulfate fractionation, sucrose gradient centrifugation, salf gradient elution from DEAE-cellulos
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8. S-nitrosoprotein formation and localization in endothelial cells
Protein S-nitrosation represents a recently described form of post-translational modification that is rapid and reversible. However, the analysis of protein S-nitrosation in situ has been difficult because of the absence of specific probes and the instability of cellular protein S-nitrosothiols. We developed a rapid and specific method for detecting endothel
National Academy of Sciences.
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9. Aflatoxin B1 dihydrodiol antibody: production and specificity.
A specific antibody for 2,3-dihydro-2,3-dihydroxyaflatoxin B1 (AFB1-diol) was prepared, and its reactivity was characterized for the major aflatoxin (AF) B1 (AFB1) metabolites. Reductive alkylation was used to conjugate AFB1-diol to ethylenediamine-modified bovine serum albumin (EDA-BSA) and horseradish peroxidase for use as an immunogen and an enzyme-linked