Results 151 to 160 of about 4,480 (203)
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1994
Abstract a-Mannosidase II was originally detected in rat liver Golgi membrane fractions, using p-nitrophenyl-a-D-mannoside as substrate1, as an activity distinct from the lysosomal and soluble a-mannosidases2. The enzyme was subsequently shown to have an extremely restricted specificity toward natural oligosaccharide substrates, removing
R Trimble, K Moremen,, A Herscovics
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Abstract a-Mannosidase II was originally detected in rat liver Golgi membrane fractions, using p-nitrophenyl-a-D-mannoside as substrate1, as an activity distinct from the lysosomal and soluble a-mannosidases2. The enzyme was subsequently shown to have an extremely restricted specificity toward natural oligosaccharide substrates, removing
R Trimble, K Moremen,, A Herscovics
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Electrophoretic heterogeneity of human α-mannosidase
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973Abstract Electrophoresis on cellulose acetate of human tissue extracts demonstrated the presence of three bands of α-mannosidase (α- d -mannoside mannohydrolase, EC 3.2.1.24) activity. One band stained at a neutral pH, the two others at an acid pH. The pattern of acid α-mannosidase was different in various tissues.
L, Poenaru, J C, Dreyfus
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Properties of α-Mannosidase in Mannosidosis
Scandinavian Journal of Clinical and Laboratory Investigation, 1970The rest activity of α-tnannosidase in a patient with mannosidosis was investigated. By isoelectric focusing both patient and controls showed heterogeneity.
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Human chorionic β‐mannosidase: Comparison with β‐mannosidase from human cultured fibroblasts
Prenatal Diagnosis, 1992AbstractThe conditions for assay of β‐mannosidase activity in human chorionic villi (CV) were studied using the fluorogenic substrate 4‐methylumbelliferyl‐β‐D‐mannopyranoside. A comparison of the biochemical properties of the CV β‐mannosidase with those of the enzyme from human cultured fibroblasts showed their similarity.
N A, Petushkova +2 more
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Alpha-Mannosidase Activity in Synovial Fluid
Scandinavian Journal of Rheumatology, 1970A microassay technique for the evaluation of synovial fluid alpha-mannosidase activity is presented with the evaluation of 184 synovial fluid samples from a variety of arthropathic conditions. The results indicate a close correlation of enzyme activity with synovial fluid cell count and the degree of inflammation associated with the various types of ...
B A, Bartholomew, A L, Perry
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Mannosidases of the Golgi complex
1994Abstract The trimming phase of the N-glycan processing pathway is initiated by a-glucosidases I and II and a collection of processing mannosidases in the ER and Golgi complex, which remove the four a1,2-mannose residues to yield Man5GlcNAc2.
R B Trimble, K Morcmcn, A Hcrscovics
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A new strong inhibitor of beta-mannosidase
Bioorganic & Medicinal Chemistry Letters, 1998N-phenyl-carbamate of D-mannonohydroxymolactone (I) was synthesized from mannose and was shown to be the best competitive inhibitor of beta-mannosidase so far reported (Ki = 25 nM).
H, Therisod, Y, Letourneux, M, Therisod
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α-Mannosidase from the Seeds of Triticale
The Journal of Biochemistry, Molecular Biology and Biophysics, 2002Seeds of Triticale (hybrid of wheat and rye) contain an N-acetylglucosamine specific lectin that was affinity purified in our laboratory (Siva Kumar, N. and Padma, K. (1996) "Affinity purification of N-acetyl glucosamine specific lectin. Purification and partial characterization of Triticale lectin". Biochem. Mol. Biol. Int. 38, 1059-1066).
A, Subha Mahadevi +2 more
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2002
Golgi α-mannosidase II (MII) is a processing enzyme involved in N-glycan biosynthesis (Tulsiani et al. 1982b; Moremen and Touster 1985; Moremen et al. 1994). Mil- related enzyme, α-mannosidase IIx (MX), was identified in the human genome; and subsequently, MX cDNA was cloned (Misago et al. 1995).
Tomoya O. Akama +2 more
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Golgi α-mannosidase II (MII) is a processing enzyme involved in N-glycan biosynthesis (Tulsiani et al. 1982b; Moremen and Touster 1985; Moremen et al. 1994). Mil- related enzyme, α-mannosidase IIx (MX), was identified in the human genome; and subsequently, MX cDNA was cloned (Misago et al. 1995).
Tomoya O. Akama +2 more
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Microbial β-mannosidases and their industrial applications
Applied Microbiology and Biotechnology, 2018Heteropolymers of mannan are polysaccharide components of the plant cell wall of gymnosperms and some angiosperms, including palm trees (Arecales and Monocot). Degradation of the complex structure of these polysaccharides requires the synergistic action of enzymes that disrupt the internal carbon skeleton of mannan and accessory enzymes that remove ...
Diandra Albuquerque Lopes Costa +1 more
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