Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum.

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Lysosomal Enzyme Precursors in Human Fibroblasts. Activation of Cathepsin D Precursor in vitro and Activity of beta-Hexosaminidase A Precursor towards Ganglioside GM2

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Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.

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Convenient and quantitative determination of the frequency of a mutant allele using solid-phase minisequencing: Application to aspartylglucosaminuria in Finland

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Studies on Enzymes Acting on Glycopeptides*

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Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum.

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In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation

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The amino-terminal sequences in the pro-α and -β polypeptides of human lysosomal β-hexosaminidase A and B are retained in the mature isozymes

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Isolation of a human hepatic 60 kDa aspartylglucosaminidase consisting of three non-identical polypeptides

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Deletion of the 3'-untranslated region of aspartylglucosaminidase mRNA results in a lysosomal accumulation disease.

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