Results 161 to 170 of about 4,480 (203)
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β‐Mannosidase in human leukocytes and fibroblasts
Journal of Inherited Metabolic Disease, 1984AbstractIn human leukocytes and fibroblasts β‐mannosidase activity has a unimodal pH optimum (4.0–4.5). Markedly reduced activity is found in I‐cell disease. Normal activities in human fibroblasts are ten times higher than in the goat, in which species a deficiency disease has been described.
R S, Panday +3 more
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β-Mannosidase from Thermotoga species
2001Publisher Summary β -Mannosidase is an exo-acting glycosylhydrolase whose function is to cleave mannose residues from the nonreducing termini of mannan oligosaccharides. In microorganisms, β -mannosidases often act in concert with endo-acting β -mannanases to completely hydrolyze mannan-based carbohydrates to be subsequently used for nutritional ...
K N, Parker +5 more
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Mitogenic effect of α-mannosidase on lymphocytes
Nature, 1978MITOGENS induce blastogenesis and mitosis in lymphocytes after reacting with specifie receptors on the cell surface. In contrast to antigen receptors, the receptors for mitogens may be common to large fractions of the lymphocyte population. For example, the lectin concanavalin A (con A) causes mitosis in most T cells.
E, Paus, H B, Steen
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Origin of α-mannosidase activity in CSF
The International Journal of Biochemistry & Cell Biology, 2017The α-mannosidase activity in human frontal gyrus, cerebrospinal fluid and plasma has been analyzed by DEAE-cellulose chromatography to investigate the origin of the α-mannosidase activity in cerebrospinal fluid (CSF). The profile of α-mannosidase isoenzymes obtained in CSF was similar to that in the frontal gyrus but different from that in human ...
Tasegian, Anna +10 more
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1973
Publisher Summary This chapter discusses that there are two attributes of α -D-mannosidase, which receive particular attention—namely, its behavior as a zinc-containing metalloenzyme, and its action on naturally occurring, D-mannose-containing molecules. The wide occurrence of α -D-mannosidase as compared to that of β-D-mannosidase suggested that, as
Sybil M. Snaith, Guildford A. Levvy
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Publisher Summary This chapter discusses that there are two attributes of α -D-mannosidase, which receive particular attention—namely, its behavior as a zinc-containing metalloenzyme, and its action on naturally occurring, D-mannose-containing molecules. The wide occurrence of α -D-mannosidase as compared to that of β-D-mannosidase suggested that, as
Sybil M. Snaith, Guildford A. Levvy
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α-Mannosidase as a Zinc-dependent Enzyme
Nature, 1968CADMIUM has been reported to have a teratogenic effect in the golden hamster1, which is reversed by zinc. This prompts us to draw attention to our recent observation2 that zinc is an essential component of α-mannosidase. The active zinc–protein complex is readily dissociable at pH 5, the pH of optimum enzyme activity and the zinc ion can be displaced ...
S M, Snaith, G A, Levvy
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In Vitro Mannosidase Assay of EDEMs: ER Degradation-Enhancing α-Mannosidase-Like Proteins
2020Quality control of newly synthesized glycoproteins is tightly regulated by sugar processing of N-glycans and by recognition of specific glycan structures by lectins in the endoplasmic reticulum (ER). Mannose trimming and its recognition determine the targeting of misfolded glycoproteins for ER-associated degradation.
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The soluble α-mannosidases of Drosophila melanogaster
Insect Biochemistry and Molecular Biology, 1997The alpha-mannosidases are implicated in both the catabolism of carbohydrates and the N-linked glycosylation pathway in insects, but little is known of the biochemistry of these glycosidases. In order to study the soluble alpha-mannosidases of Drosophila melanogaster we have used artificial fluorogenic substrates for detection of activity in situ ...
J M, Foster, D B, Roberts
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Characterization of α‐mannosidase in feline mannosidosis
Journal of Inherited Metabolic Disease, 1987AbstractAcidic α‐mannosidase deficiency has been identified in a family of Blue Persian cats. Characterization of the residual activity revealed that theKm for the substrate, 4‐methylumbelliferyl‐α‐d‐mannoside, increased approximately three‐fold with a severe deficiency inVmax (1–2%) in homogenates of liver and brain of affected cats compared with ...
S, Raghavan +4 more
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Archives of Biochemistry and Biophysics, 1996
Studies were undertaken to evaluate the relationship of the recently described (S. Weng and R. G. Spiro, 1993, J. Biol. chem. 268, 25656-25663) rat liver kifunensine (KIF)-resistant mannosidase (ER mannosidase II) to the mannose-trimming enzyme of cytosol.
S, Weng, R G, Spiro
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Studies were undertaken to evaluate the relationship of the recently described (S. Weng and R. G. Spiro, 1993, J. Biol. chem. 268, 25656-25663) rat liver kifunensine (KIF)-resistant mannosidase (ER mannosidase II) to the mannose-trimming enzyme of cytosol.
S, Weng, R G, Spiro
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