Results 161 to 170 of about 7,225 (221)

Hexosaminidase assays

Glycoconjugate Journal, 2008
beta-Hexosaminidases (EC 3.2.1.52) are lysosomal enzymes that remove terminal beta-glycosidically bound N-acetylglucosamine and N-acetylgalactosamine residues from a number of glycoconjugates. Reliable assay systems are particularly important for the diagnosis of a family of lysosomal storage disorders, the GM2 gangliosidoses that result from inherited
Michaela, Wendeler, Konrad, Sandhoff
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Anchimeric assistance in hexosaminidases

Canadian Journal of Chemistry, 2002
Configuration retaining glycosidases catalyse the hydrolysis of glycosidic bonds via a double displacement mechanism, typically involving two key active site carboxyl groups (Glu or Asp). One of the enzymic carboxyl groups functions as a general acid–base catalyst, the other acts as a nucleophile. Alternatively, configuration-retaining hexosaminidases
B. Mark, M. James
semanticscholar   +2 more sources

The tissue distribution of hexosaminidase S and hexosaminidase C

Annals of Human Genetics, 1977
SUMMARYThe proportion of hex S to hex C in normal and Sandhoff's fibroblasts was determined to be between 1:1 and 1:2 by differential staining of hex S at pH 4.4 with 4‐methylumbelliferyl‐β‐N‐acetylgalactosaminide and of hex C at pH 7.0 with 4‐methylumbelliferyl‐β‐N‐acetylglucosaminide.
E, Beutler, W, Kuhl
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Affinity purification of hexosaminidases

Journal of Biochemical and Biophysical Methods, 1987
Hexosaminidases A and B were purified by affinity chromatography from normal gastric mucosa, after preliminary separation of isozymes by anion exchange chromatography. Heparin and mannosamine were coupled to Sepharose 4B and used as affinity matrices and the purified enzymes were found to be homogeneous when analysed by polyacrylamide slab gel ...
P, Sankaranarayanan, S, Chandrasekaran, R, Puvanakrishnan, S C, Dhar, S, Gopalakrishnan, N, Rangabashyam   +5 more
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Subunit structure of human hexosaminidase verified: interconvertibility of hexosaminidase isozymes

Nature, 1975
Two major and several minor isozymes of hexosaminidase (Hex) exist in human tissues. In Tay-Sachs disease Hex A is missing but the activity of Hex B is increased. In Sandhoff's disease, both Hex A and Hex B are lacking; the residual activity represents increased amounts of a normal minor isozyme, Hex S.
E, Beutler, W, Kuhl
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Serum β-hexosaminidases in pregnancy

Clinica Chimica Acta, 1979
Serum contains several hexosaminidase forms. Two, HEX A and HEX B, migrate in both DEAE cellulose and isoelectric focussing systems like their tissue counterparts. A major group of serum hexosaminidases migrate in an intermediate position. These forms, collectively named HEX 1, increase during pregnancy and obscure carrier detection for Tay-Sachs and ...
J. Lowden
semanticscholar   +3 more sources

Hexosaminidases: Multiple Component Enzymes

1976
In 1968 Robinson and Stirling (1) demonstrated that lysosomal N-acetylhexosaminidase could be separated into two species by starch gel electrophoresis. They noted that the more anodic form, A, was heat-labile and that it could be converted to the less anodic form, B, by the action of neuraminidase.
J A, Lowden, J W, Callahan, F N, Howard
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Hexosaminidase A deficiency in adults

American Journal of Medical Genetics, 1986
AbstractDeficiency of hexosaminidase A (Hex A) in adults was found in 15 individuals from nine unrelated Ashkenazi families; 14 individuals had neurological symptoms, one was clinically intact. Clinical, biochemical and genetic findings are reported and compared to previously reported cases.The clinical picture varied between and within families and ...
Ruth Navon, Zohar Argov, Amos Frisch, John M. Opitz, James F. Reynolds   +4 more
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Differential inhibition of β-hexosaminidase A and β-hexosaminidase B by suramin

Biochemical and Biophysical Research Communications, 1981
Abstract The trypanocidal drug suramin is a potent inhibitor of β-hexosaminidase A with a K i of about 4.5 μM, and to a lesser extent of β-hexosaminidase B (K i 31.5 μM). β-Hexosaminidase B remained active in the presence of 1.0 mM suramin whereas the activity of β-hexosaminidase A was completely inhibited at 0.1 mM.
G, Constantopoulos, S, Rees, B G, Cragg, J A, Barranger, R O, Brady   +4 more
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Antibody against purified human hexosaminidase B cross-reacting with human hexosaminidase A

Biochemical and Biophysical Research Communications, 1972
Abstract Human hexosaminidase B has been purified to virtually homogeneous state from placenta. An anti-serum has been prepared in rabbits against the purified preparation. The serum reacted equally with human hexosaminidase B (free of hexosaminidase A) and with human hexosaminidase A (free of hexosaminidase B) as shown by immunodiffusion and by ...
S K, Srivastava, E, Beutler
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