منابع مشابه
Structure of the lysosomal neuraminidase-beta-galactosidase-carboxypeptidase multienzymic complex.
Lysosomal neuraminidase (sialidase; EC 3.2.1.18) and beta-galactosidase (EC 3.2.1.23), together with a carboxypeptidase, the so-called 'protective protein', were co-purified from the human placenta by affinity chromatography on a concanavalin A-Sepharose column followed by a thiogalactoside-agarose affinity column for beta-galactosidase. Analysis of the purified material by gel-filtration h.p.l...
متن کاملPhotoaffinity labeling of the lysosomal neuraminidase from bovine testis.
ASA-NeuAc2en, a photoreactive arylazide derivative of sialic acid, is shown to be a powerful competitive inhibitor of lysosomal neuraminidase from bovine testis (Ki approximately 21 microM). Photoaffinity labeling and partial purification of preparations containing this lysosomal neuraminidase activity result in specifically and non-specifically labeled polypeptides. Only labeling in a 55 kDa p...
متن کاملTransport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A.
Human lysosomal N-acetyl-alpha-neuraminidase is deficient in two lysosomal storage disorders, sialidosis, caused by structural mutations in the neuraminidase gene, and galactosialidosis, in which a primary defect of protective protein/cathepsin A (PPCA) leads to a combined deficiency of neuraminidase and beta-D-galactosidase. These three glycoproteins can be isolated in a high molecular weight ...
متن کاملCharacterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis.
Neuraminidases (sialidases) have an essential role in the removal of terminal sialic acid residues from sialoglycoconjugates and are distributed widely in nature. The human lysosomal enzyme occurs in complex with beta-galactosidase and protective protein/cathepsin A (PPCA), and is deficient in two genetic disorders: sialidosis, caused by a structural defect in the neuraminidase gene, and galact...
متن کاملNovel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis.
Lysosomal neuraminidase is the key enzyme for the intralysosomal catabolism of sialylated glycoconjugates and is deficient in two neurodegenerative lysosomal disorders, sialidosis and galactosialidosis. Here we report the identification of eight novel mutations in the neuraminidase gene of 11 sialidosis patients with various degrees of disease penetrance. Comparison of the primary structure of ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.m007380200