Biomaterial Database

Purification of some glycoside hydrolases by affinity chromatography. 1977

M Edward, and R J Sturgeon

Two glycoproteins have been isolated from the cell walls of baker's yeast. One is a glucan-protein complex which has been partially characterised as having a branched carbohydrate structure composed of chains of (1 leads to 3)-linked beta-D-glucosyl residues, some of which are attached by (1 leads to 6)-linkages to the main chain. Immobilization of this glycoprotein was achieved by covalent attachment to Sepharose, and the product was used to isolate a number of (1 leads to 3)-beta-D-glucan hydrolases from Helix pomatia, malted barley, and Basidiomycete QM806. The second glycoprotein, a mannan-protein complex, after immobilization, has been used in the purification of an alpha-D-mannosidase from jack-bean meal.

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
D010944	Plants	Multicellular, eukaryotic life forms of kingdom Plantae. Plants acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations. It is a non-taxonomical term most often referring to LAND PLANTS. In broad sense it includes RHODOPHYTA and GLAUCOPHYTA along with VIRIDIPLANTAE.	Plant
D002846	Chromatography, Affinity	A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D004693	Glucan Endo-1,3-beta-D-Glucosidase	An endocellulase with specificity for the hydrolysis of 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans including laminarin, paramylon, and pachyman.	Endo-1,3-beta-Glucanase,Oligo-1,3-Glucosidase,Zymolase,Endo 1,3 beta Glucanase,Endo-1,3-beta-D-Glucosidase, Glucan,Glucan Endo 1,3 beta D Glucosidase,Oligo 1,3 Glucosidase
D006023	Glycoproteins	Conjugated protein-carbohydrate compounds including MUCINS; mucoid, and AMYLOID glycoproteins.	C-Glycosylated Proteins,Glycosylated Protein,Glycosylated Proteins,N-Glycosylated Proteins,O-Glycosylated Proteins,Glycoprotein,Neoglycoproteins,Protein, Glycosylated,Proteins, C-Glycosylated,Proteins, Glycosylated,Proteins, N-Glycosylated,Proteins, O-Glycosylated
D006026	Glycoside Hydrolases	Any member of the class of enzymes that catalyze the cleavage of the glycosidic linkage of glycosides and the addition of water to the resulting molecules.	Endoglycosidase,Exoglycosidase,Glycohydrolase,Glycosidase,Glycosidases,Glycoside Hydrolase,Endoglycosidases,Exoglycosidases,Glycohydrolases,Hydrolase, Glycoside,Hydrolases, Glycoside
D006372	Helix, Snails	A genus of chiefly Eurasian and African land snails including the principal edible snails as well as several pests of cultivated plants.	Helix (Snails),Snails Helix
D000118	Acetylglucosaminidase	A beta-N-Acetylhexosaminidase that catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structural studies on bacterial cell walls and in the study of diseases such as MUCOLIPIDOSIS and various inflammatory disorders of muscle and connective tissue.	N-Acetyl-beta-D-glucosaminidase,Chitobiase,N,N-Diacetylchitobiase,N-Ac-beta-Glucosaminidase,NAGase,beta-D-Acetamido-2-Deoxyglucosidase,beta-D-N-acetylglucosaminidase,beta-N-Acetylglucosaminidase,N Ac beta Glucosaminidase,N Acetyl beta D glucosaminidase,N,N Diacetylchitobiase,beta D Acetamido 2 Deoxyglucosidase,beta D N acetylglucosaminidase,beta N Acetylglucosaminidase
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