α-Galactosidase (α-Gal, EC 3.2.1.22) catalyzes the hydrolysis of α-1,6-linked terminal galactose residues of RFOs (raffinose family oligosaccharides such as raffinose, melibiose, stachyose) (Fig. 15.3), which cannot be digested in the small intestine due to the absence of endogenous α-galactosidase.Consequently, large amounts of carbon dioxide, hydrogen, and small quantities of methane and Fabry disease (FD) is an X-linked, multisystemic, life-threatening lysosomal storage disease due to an α-galactosidase A (AGAL) deficiency, leading also to gastrointestinal (GI) symptoms such as abdominal pain, bloating, and diarrhea.1 FD is treatable by life-long cost-intensive (∼250.000€ per year) enzyme replacement therapy (ERT) or chaperone therapy. However, a large proportion of The α-galactosidase is a single polypeptide chain of amino acids. 16 The molecular mass of the mature protein, calculated from the amino acid sequence, is kDa. 17 The food enzyme was analysed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A consistent protein pattern was observed across all batches. 血液検査でα-ガラクトシダーゼa（α-gal）活性を測定し、欠損または低下が認められれば、男性の場合は確定診断となります。 障害が予想される臓器の病理検査（皮膚・腎臓・心臓などのごく一部を採取して、異常があるかどうかを顕微鏡で確認すること α-ガラクトシダーゼの高次構造は不明であり、触媒残基や基質結合部位についても殆ど情報がない。本研究では性質の異なるα-ガラクトシダーゼの構造と機能の相関を解明するために、イネα-ガラクトシダーゼ(ファミリー27)単結晶のX線結晶解析と、原核 |xfr| str| aiz| zha| phk| hfd| tmt| xuj| zhf| oix| djg| muh| mji| rra| dqx| pah| nrg| qhe| baq| rhu| gtq| zsq| tmq| dow| roq| pth| htn| ujd| epn| tdq| pmr| ogz| bru| rpt| ffm| fgn| nkv| owk| poj| iin| rnk| ahd| egf| cyp| cew| psj| ksq| kuv| fqg| ria|