RESUMEN
The uranium enrichment of the environmental sample should be analyzed to verify the declared information for the nuclear safeguards. The High-Resolution Gamma Spectrometry (HRGS) and Monochromatic Micro X-ray Fluorescence (MMXRF) is able to analyze the sample with a short detection time and high reproducibility. These are the advantage to measure the samples for screening before laboratory analysis. This study concentrated on uranium enrichment evaluation with the gamma-ray emission counts of 235U isotope (@185.7â¯keV) detected with the HRGS and counts of total uranium elements detected by MMXRF. As a result, the measured data were calculated for the uranium enrichment in three different ways: (i) Activity of 235U with the HRGS and mass of total uranium with the MMXRF, (ii) counts 235U with the HRGS and counts of total uranium, and (iii) activity of 235U and 238U with the HRGS. Based on the comparison with the mass spectrometry, method (iii) is able to derive the uranium enrichment the most accurately. However, method (ii) provides enough information for the screening to sort the sample for which laboratory analysis is necessary, when the sample's equilibrium status is not guaranteed.
RESUMEN
AB204 is an Activin/BMP2 chimera, which has been found to exhibit a higher activity than Bone Morphogenetic Protein 2 (BMP2) in osteogenic activity. To prepare AB204 for its preclinical studies, AB204 has been characterized in various formulation buffers. We observed that AB204 purified by ion-exchange chromatography has low water solubility (2.0 mg/ml), whereas it has high water solubility (higher than 10.0 mg/ml) when purified by reverse-phase chromatography. Analysis of the purification procedures reveals that the buffer composition at the lyophilization step determines the solubility. Lyophilization from sodium acetate buffer at pH 4.5 resulted in formation of sodium hydroxide, which caused low solubility of AB204 by pH increase upon reconstitution in water. However, lyophilization from buffers, containing acetic acid or trifluoroacetic acid (TFA) rendered AB204 to be highly soluble. During the course of these analyses, we found a simple procedure to further reduce residual amount of TFA in the purified AB204.
Asunto(s)
Activinas/genética , Activinas/aislamiento & purificación , Proteína Morfogenética Ósea 2/genética , Proteína Morfogenética Ósea 2/aislamiento & purificación , Activinas/química , Animales , Proteína Morfogenética Ósea 2/química , Línea Celular , Cromatografía por Intercambio Iónico , Cromatografía de Fase Inversa , Humanos , Ratones , Resonancia Magnética Nuclear Biomolecular , Proteínas Recombinantes de Fusión/química , Proteínas Recombinantes de Fusión/genética , Proteínas Recombinantes de Fusión/aislamiento & purificación , SolubilidadRESUMEN
A beta-glucosidase from Phoma sp. KCTC11825BP isolated from rotten mandarin peel was purified 8.5-fold with a specific activity of 84.5 U/mg protein. The purified enzyme had a molecular mass of 440 kDa with a subunit of 110 kDa. The partial amino acid sequence of the purified beta-glucosidase evidenced high homology with the fungal beta- glucosidases belonging to glycosyl hydrolase family 3. Its optimal activity was detected at pH 4.5 and 60 degrees C, and the enzyme had a half-life of 53 h at 60 degrees C. The Km values for p-nitrophenyl-beta-D-glucopyranoside and cellobiose were 0.3 mM and 3.2 mM, respectively. The enzyme was competitively inhibited by both glucose (Ki=1.7 mM) and glucono-delta-lactone (Ki=0.1 mM) when pNPG was used as the substrate. Its activity was inhibited by 41% by 10 mM Cu2+ and stimulated by 20% by 10 mM Mg2+.
Asunto(s)
Ascomicetos/enzimología , Citrus sinensis/microbiología , Proteínas Fúngicas/química , Proteínas Fúngicas/aislamiento & purificación , beta-Glucosidasa/química , beta-Glucosidasa/aislamiento & purificación , Ascomicetos/clasificación , Ascomicetos/genética , Ascomicetos/aislamiento & purificación , Citrus sinensis/química , Estabilidad de Enzimas , Proteínas Fúngicas/genética , Proteínas Fúngicas/metabolismo , Cinética , Datos de Secuencia Molecular , Peso Molecular , Filogenia , Especificidad por Sustrato , beta-Glucosidasa/genética , beta-Glucosidasa/metabolismoRESUMEN
A total of 1,044 school children identified with hematuria and/or proteinuria during a mass school urine screening test were referred to pediatric nephrologists at 13 hospitals in Korea. These children had isolated hematuria (IH) (60.1%), isolated proteinuria (IP) (26.4%: transient, 19.6%; orthostatic, 4.9%; persistent, 1.9%) or combined hematuria and proteinuria (CHP) (13.5%). The patient's history, physical examination, laboratory tests, kidney ultrasound and Doppler ultrasonography were obtained. Renal biopsies were performed on 113 children who showed severe proteinuria, hypertension, abnormal renal function, family history of chronic renal disease, systemic diseases or persistent hematuria and/or proteinuria for more than 12 months. IgA nephropathy (IgAN), thin basement membrane nephropathy (TBMN), membranoproliferative glomerulonephritis (MPGN), focal segmental glomerulosclerosis (FSGS), other GN, Alport syndrome and lupus nephritis were detected. IgAN and TBMN were the most common causes in the CHP group and IH group, respectively. Abnormal findings on the renal ultrasound with or without Doppler ultrasonography were noted in 147 cases (suspected nutcracker phenomenon, 65; increased parenchymal echogenicity, 40; hydronephrosis, 15). This study showed that the use of a mass school urine screening program can detect chronic renal disease in its early stage and recommends that more attention should be paid to identifying those children with CHP and massive proteinuria. A school urine screening program can detect chronic renal disease in its early stage. When mass screening is used, the initial aggressive diagnostic procedures such as renal biopsy are not needed. In addition, a regular follow-up for those children with IH and IP is certainly warranted.