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3.2.1.22

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Showing 1-18 of 18 results for "3.2.1.22 " within Papers
F J Novo et al.
Nucleic acids research, 23(14), 2636-2640 (1995-07-25)
During a study of the gene coding for alpha-galactosidase (EC 3.2.1.22), the lysosomal enzyme deficient in Fabry's disease, RT-PCR amplification of alpha-galactosidase mRNAs obtained from three different tissues isolated from males revealed a substantial number of clones with a U
Christine R Kaneski et al.
Molecular genetics and metabolism, 119(1-2), 144-150 (2016-07-30)
Fabry disease is a glycosphingolipid storage disorder that is caused by a genetic deficiency of the enzyme alpha-galactosidase A (AGA, EC 3.2.1.22). It is a multisystem disease that affects the vascular, cardiac, renal, and nervous systems. One of the hallmarks
L C Blanch et al.
Human mutation, 8(1), 38-43 (1996-01-01)
Fabry disease is an X-linked recessive lysosomal storage disorder caused by a deficiency of alpha-galactosidase A (alpha-gal; EC 3.2.1.22). In the past, it has been difficult to give an unequivocal diagnosis of carrier status in Fabry disease because of the
Masaaki Shimotori et al.
Human mutation, 29(2), 331-331 (2008-01-22)
Fabry disease is an X-linked recessive inborn metabolic disorder caused by a deficiency of the lysosomal enzyme alpha-galactosidase A (EC 3.2.1.22). The causative mutations are diverse, include both large rearrangements and single-base substitutions, and are dispersed throughout the 7 exons
Ivan B Tomasic et al.
The Journal of biological chemistry, 285(28), 21560-21566 (2010-05-07)
The human lysosomal enzymes alpha-galactosidase (alpha-GAL, EC 3.2.1.22) and alpha-N-acetylgalactosaminidase (alpha-NAGAL, EC 3.2.1.49) share 46% amino acid sequence identity and have similar folds. The active sites of the two enzymes share 11 of 13 amino acids, differing only where they
D F Bishop et al.
The Journal of biological chemistry, 256(3), 1307-1316 (1981-02-10)
The substrate analog alpha-D-galactosylamine was synthesized, linked to 6-aminohexanoic acid, and coupled to carboxyhexyl-Sepharose. This affinity support permitted the purification of human alpha-galactosidase A (alpha-D-galactoside galactohydrolase, EC 3.2.1.22) from spleen, placenta, and plasma. When used in conjunction with conventional procedures
Seçil Onal et al.
Artificial cells, blood substitutes, and immobilization biotechnology, 31(3), 339-355 (2003-08-09)
alpha-Galactosidase (alpha-D-galactoside galactohydrolase, EC 3.2.1.22) from watermelon was covalently immobilized on chitin. The immobilized alpha-galactosidase exhibited an activity of 0.61 U per g of carrier and an activity yield of 67%. The properties of free and immobilized alpha-galactosidase were also
T Ohshima et al.
Gene, 166(2), 277-280 (1995-12-12)
alpha-Galactosidase A (alpha-D-galactoside galactohydrolase, EC 3.2.1.22; alpha GalA) is a lysosomal enzyme that hydrolyses the alpha-D-galactosyl residues from glycosphingolipids. Fabry disease, an inhibited X-linked recessive human metabolic disorder, results from a mutation in the alpha GalA gene at Xq22. As
Chin-Pin Soh et al.
Phytochemistry, 67(3), 242-254 (2005-12-06)
alpha-Galactosidase (EC 3.2.1.22) from ripe papaya (Carica papaya L.) fruit was fractionated by a combination of ion exchange and gel filtration chromatography into three forms, viz., alpha-galactosidase 1, 2 and 3. The predominant isoform, alpha-gal 2, was probably a tetramer
D F Bishop et al.
Proceedings of the National Academy of Sciences of the United States of America, 83(13), 4859-4863 (1986-07-01)
The complete nucleotide sequence has been determined for a lambda gt11 cDNA clone (lambda AG18) containing the full-length coding region for the mature lysosomal form of human alpha-galactosidase A (alpha-Gal A; EC 3.2.1.22). The lambda AG18 insert contained a 1226-base-pair
Abigail I Guce et al.
The Journal of biological chemistry, 285(6), 3625-3632 (2009-11-27)
The enzyme alpha-galactosidase (alpha-GAL, also known as alpha-GAL A; E.C. 3.2.1.22) is responsible for the breakdown of alpha-galactosides in the lysosome. Defects in human alpha-GAL lead to the development of Fabry disease, a lysosomal storage disorder characterized by the buildup
Y A Ioannou et al.
The Biochemical journal, 332 ( Pt 3), 789-797 (1998-06-11)
Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined. Endoglycosidase treatment
D F Bishop et al.
Proceedings of the National Academy of Sciences of the United States of America, 85(11), 3903-3907 (1988-06-01)
Human alpha-galactosidase A (alpha-D-galactoside galactohydrolase; EC 3.2.1.22) is a lysosomal hydrolase encoded by a gene localized to the chromosomal region Xq22. The deficient activity of this enzyme results in Fabry disease, an X chromosome-linked recessive disorder that leads to premature
A K Topaloglu et al.
Molecular medicine (Cambridge, Mass.), 5(12), 806-811 (2000-02-10)
Fabry disease, an X-linked inborn error of glycosphingolipid catabolism, results from the deficient activity of the lysosomal exoglycohydrolase alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A). The nature of the molecular lesions in the alpha-Gal A gene in 30 unrelated families was
R W Gotlib et al.
Biochemical and molecular medicine, 57(2), 139-148 (1996-04-01)
The full-length cDNA and genomic sequences encoding mouse alpha-galactosidase A (alpha-Gal A; EC 3.2.1.22), a lysosomal galactohydrolase, were isolated and characterized. The cDNA's open reading frame encoded 419 amino acids and had 82% nucleotide (nt) and 78% amino acid identity
Gao et al.
Plant physiology, 119(3), 979-988 (1999-03-09)
The cucurbits translocate the galactosyl-sucrose oligosaccharides raffinose and stachyose, therefore, alpha-galactosidase (alpha-D-galactoside galactohydrolase, EC 3.2.1.22) is expected to function as the initial enzyme of photoassimilate catabolism. However, the previously described alkaline alpha-galactosidase is specific for the tetrasaccharide stachyose, leaving raffinose
R Kornreich et al.
The Journal of biological chemistry, 265(16), 9319-9326 (1990-06-05)
Fabry disease, an inborn error of glycosphingolipid catabolism, results from mutations in the X-linked gene encoding the lysosomal enzyme, alpha-galactosidase A (EC 3.2.1.22). Six alpha-galactosidase A gene rearrangements that cause Fabry disease were investigated to assess the role of Alu
Junaid Shabbeer et al.
Human genomics, 2(5), 297-309 (2006-04-06)
Fabry disease, an X-linked recessive inborn error of glycosphingolipid catabolism, results from the deficient activity of the lysosomal exoglycohydrolase, alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A). The molecular lesions in the alpha-Gal A gene causing the classic phenotype of Fabry disease
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