کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9229626 | 1203317 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Three dimensional structural studies of α-N-acetylgalactosaminidase (α-NAGA) in α-NAGA deficiency (Kanzaki disease): different gene mutations cause peculiar structural changes in α-NAGAs resulting in different substrate specificities and clinical phen
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم پزشکی و سلامت
پزشکی و دندانپزشکی
امراض پوستی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Our findings suggest that the association of α-NAGA with its substrates is strongly affected by the amino acid substitution at R329 and that the association with GalNAcα1-O-Thr is more highly susceptible to structural changes. The residual mutant enzyme in R329W could not associate with GalNAcα1-O-Thr and GalNAcα1-O-Ser. However, the residual mutant enzyme in R329Q catalyzed GalNAcα1-O-Ser to some extent. Therefore, the urinary ratio of GalNAcα1-O-Ser:GalNAcα1-O-Thr was lower and the clinical phenotype was milder in the R329Q mutation. Structural analysis revealed biochemical and phenotypic differences in these Kanzaki patients with the R329Q and R329W mutation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Dermatological Science - Volume 37, Issue 1, January 2005, Pages 15-20
Journal: Journal of Dermatological Science - Volume 37, Issue 1, January 2005, Pages 15-20
نویسندگان
Takuro Kanekura, Hitoshi Sakuraba, Fumiko Matsuzawa, Seiichi Aikawa, Hirofumi Doi, Yoshio Hirabayashi, Noriko Yoshii, Tomoko Fukushige, Tamotsu Kanzaki,