Purification and characterization of an alpha-mannosidase of sea-squirt. 1983

S Shigeta, and H Kubota, and H Tamura, and S Oka

An alpha-mannosidase was isolated from the extract of acetone powder of CHCl3-treated internal organs of the sea-squirt, Styela plicata. The enzyme was purified 4,110-fold in 11% yield. The preparation was fairly homogeneous on disc and SDS-polyacrylamide gel electrophoreses and Sephadex G-200 chromatography. The enzyme had an estimated molecular weight of 275,000 by gel chromatography and 70,000 by SDS-polyacrylamide gel electrophoresis, and was therefore considered to be a tetramer. The optimum pH for the enzyme activity was 3.4 but the stable pH range was from 4 to 6. The isoelectric point was 5.0. The enzyme was activated by Zn2+ but inhibited by Cu2+, Fe2+, Hg2+, and EDTA. The isolated enzyme released mannose not only from stem bromelin glycopeptide and ovalbumin glycopeptide but also from yeast mannan.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008361 Mannosidases Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE. Mannosidase
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D002413 Cations, Divalent Positively charged atoms, radicals or groups of atoms with a valence of plus 2, which travel to the cathode or negative pole during electrolysis. Divalent Cations
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D014561 Urochordata A subphylum of chordates intermediate between the invertebrates and the true vertebrates. It includes the Ascidians. Ascidia,Tunicata,Ascidiacea,Ascidians,Sea Squirts,Tunicates,Urochordates,Ascidian,Sea Squirt,Squirt, Sea,Tunicate,Urochordate
D043323 alpha-Mannosidase An enzyme that catalyzes the HYDROLYSIS of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. The enzyme plays a role in the processing of newly formed N-glycans and in degradation of mature GLYCOPROTEINS. There are multiple isoforms of alpha-mannosidase, each having its own specific cellular location and pH optimum. Defects in the lysosomal form of the enzyme results in a buildup of mannoside intermediate metabolites and the disease ALPHA-MANNOSIDOSIS. Lysosomal alpha-Mannosidase,LAMAN,Neutral alpha-Mannosidase,alpha Mannosidase B,alpha-D-Mannosidase,alpha-D-Mannoside Mannohydrolase,Lysosomal alpha Mannosidase,Mannohydrolase, alpha-D-Mannoside,Mannosidase B, alpha,Neutral alpha Mannosidase,alpha D Mannosidase,alpha D Mannoside Mannohydrolase,alpha Mannosidase,alpha-Mannosidase, Lysosomal,alpha-Mannosidase, Neutral
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular

Related Publications

S Shigeta, and H Kubota, and H Tamura, and S Oka
January 2000, Journal of bioscience and bioengineering,
S Shigeta, and H Kubota, and H Tamura, and S Oka
July 1991, Journal of biochemistry,
S Shigeta, and H Kubota, and H Tamura, and S Oka
July 1982, Journal of biochemistry,
S Shigeta, and H Kubota, and H Tamura, and S Oka
February 1972, European journal of biochemistry,
S Shigeta, and H Kubota, and H Tamura, and S Oka
May 1996, Journal of biochemistry,
S Shigeta, and H Kubota, and H Tamura, and S Oka
May 2001, Molecular genetics and metabolism,
S Shigeta, and H Kubota, and H Tamura, and S Oka
September 1984, Journal of biochemistry,
S Shigeta, and H Kubota, and H Tamura, and S Oka
June 1982, Journal of biochemistry,
S Shigeta, and H Kubota, and H Tamura, and S Oka
January 1982, Enzyme,
S Shigeta, and H Kubota, and H Tamura, and S Oka
July 1995, Biochimica et biophysica acta,
Copied contents to your clipboard!