6 risultati
Fibroblast cell lines obtained from five patients with the early onset form of Tay Sachs disease (TSD) possess a species of beta-N-acetylhexosaminidase (Hex) which is more anionic than Hex B but which is stable to heating under conditions which completely inactivate Hex A. This species, which
GM2 gangliosidoses, including Tay-Sachs and Sandhoff diseases, are neurodegenerative lysosomal storage diseases that are caused by deficiency of β-hexosaminidase A, which comprises an αβ heterodimer. There are no effective treatments for these diseases; however, various strategies aimed at restoring
Loss of function of the enzyme β-hexosaminidase A (HexA) causes the lysosomal storage disorder Tay-Sachs disease (TSD). It has been proposed that mutations in the α chain of HexA can impair folding, enzyme assembly, and/or trafficking, yet there is surprisingly little known about the mechanisms of
Cultured skin fibroblasts from hexosaminidase A deficient adults synthesize the alpha and beta chain precursors of beta-hexosaminidase (EC 3.2.1.30) of the same molecular weight as that synthesized by normal fibroblasts. However, the amount of the alpha chain precursor is greatly reduced. The alpha
We isolated two copia-type retrotransposons from Arabidopsis thaliana. We named these elements AtRE1 (Arabidopsis thaliana Retro Element 1) and AtRE2. Nucleotide sequence analysis revealed that both elements have long terminal repeats (LTRs), and that their internal sequences include one large open
BACKGROUND
In eukaryotes, long terminal repeat (LTR) retrotransposons such as Copia, BEL and Gypsy integrate their DNA copies into the host genome using a particular type of DDE transposase called integrase (INT). The Gypsy INT-like transposase is also conserved in the Polinton/Maverick