Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Shiao-Shek Tang"'
Autor:
Shiao-Shek Tang, Jyh-Hwa Kau, Chih-Heng Huang, Chuan-Wang Li, Cheng-Che Liu, Der-Jiang Chiao, Wen-Zhi Lin, Cheng-Cheung Chen, Jiunn-Jye Wey, Rong-Hwa Shyu, Pei-Yi Tsui
Publikováno v:
Journal of Medical Sciences. 39:217
Background and Aim: Botulinum neurotoxin Type E (BoNT/E), one of the most lethal toxin known, is the common contamination in fishery products or fish consumption that causes foodborne botulism. It is necessary to establish a sensitive and specific me
Publikováno v:
Hybridoma. 27:43-47
A sensitive and specific ELISA was developed to detect BoNT/A in biological fluids. The assay is based on the sandwich format using monoclonal antibodies (MAb) of two distinct specificities. An affinity-purified anti-BoNT/A heavy chain MAb (150-3) is
Publikováno v:
Acta Pharmacologica Sinica. 27:1238-1246
Aim: To determine the structure factors that mediate the intoxication process of botulinum neurotoxin type A (BoNT/A). Methods: Triton X-114 phase separation experiments and 1-anilino-8-naphthalene sulfonate binding assay were used to study the struc
Publikováno v:
Toxicon. 43:27-34
Our goal was to develop a sensitive method for detecting Clostridium botulinum neurotoxin type A (BoNT/A). We were able to detect BoNT/A in the femtogram (10-15 g) range using an indirect immuno-polymerase chain reaction (immuno-PCR) assay and an ind
Autor:
Shiao-Shek Tang, Gu-Gang Chang
Publikováno v:
Journal of Biochemistry. 119:1182-1188
The kinetic mechanism of the endogenous glutathione transferase (GST) activity of octopus S-crystallin was investigated by steady-state kinetics. Biphasic double-reciprocal plots were obtained for both glutathione and the hydrophobic substrate 1-chlo
Autor:
Shiao-Shek Tang, Gu-Gang Chang
Publikováno v:
Biochemical Journal. 315:599-606
Octopus glutathione transferase (GST) was enzymically active in aerosol-OT [sodium bis-(2-ethylhexyl)sulphosuccinate]/iso-octane reverse micelles albeit with lowered catalytic constant (kcat). The enzyme reaction rate was found to be dependent on the
Publikováno v:
Free Radical Biology and Medicine. 21:955-964
Glutathione transferase (GST) from octopus hepatopancreas was rapidly inactivated by micromolar concentration of Cu(II) in the presence of ascorbate at neutral pH and 0°C. Omitting the metal ion or ascorbate, or replacing the Cu(II) with Fe(II) did
Autor:
Shiao-Shek Tang, Gu-Gang Chang
Publikováno v:
Biochemical Journal. 309:347-353
The kinetic mechanism of glutathione S-transferase (GST) from Octopus vulgaris hepatopancreas was investigated by steady-state analysis. Initial-velocity studies showed an intersecting pattern, which suggests a sequential kinetic mechanism for the en
Autor:
Gu-Gang Chang, Shiao-Shek Tang
Publikováno v:
ChemInform. 27