Search results for "α galactosidase"
showing 3 items of 3 documents
Fabry disease and multiple sclerosis misdiagnosis: the role of family history and neurological signs
2018
Fabry disease (FD) is an X-linked inherited lysosomal storage disorder caused by a galactosidase A (a-gal A) deficiency. Central nervous system involvement and chronic white matter lesions are observed in both FD and multiple sclerosis (MS), which can confound the differential diagnosis. We analyzed the GLA gene, which encodes a-gal A, in 86 patients with clinical and neuroradiological findings consistent with MS to determine whether they had FD. We identified four women initially diagnosed with MS who had GLA mutations associated with FD. Our results indicate that family history besides neurological findings should be evaluated in patients with an uncertain diagnosis of MS. Also the involv…
Fluorescence and circular dichroism spectroscopy to understand the interactions between cyclodextrins and α-galactosidase from green coffee beans
2017
Abstract The potential of fluorescence measurement and circular dichroism spectroscopy (CDSP) to evaluate the interaction between cyclodextrins (CDs) (CD cavity size, concentration, pH, reaction time, and temperature as well as different side chain groups) and α-galactosidase was evaluated. A strong relationship was observed between α-galactosidase fluorescence intensity and CD cavity size, concentration, pH, reaction time, and temperature as well as different side chain groups. Therefore, it can be concluded that fluorescence intensity measurement can be a promising tool to ascertain β-CD-α-galactosidase interactions. CDSP is also an interesting tool to understand β-CD-α-galactosidase inte…
Inhibition of cyclodextrins on α-galactosidase.
2017
This work successfully investigated the effects of different influential factors and hydrophobic cavities of cyclodextrins (CDs) on α-galactosidase (α-Gal) by detecting α-Gal activity. The highest inhibitory concentration of three kinds of CDs (α-, β-, and γ-CD) on α-Gal was 10mM. Moreover, the highest inhibition of α-Gal was obtained under the following conditions: reaction time of 90min, temperature of 30°C, and pH 6.0. Compared with other CDs, β-CD showed more ability to interact with α-Gal due to its appropriate cavity geometric dimensions. From circular dichroism and nuclear magnetic resonance it was observed that β-CD changed the secondary structure of α-Gal and formed a hydrogen bond…