Biomaterial Database

Purification and characterization of two endo-beta-1,4-D-glucanases from Sclerotinia sclerotiorum. 1991

G Waksman

Department of Microbiology, University of Bristol, The Medical School, U.K.

The endo-beta-1,4-D-glucanase (EC 3.2.1.4) enzymes produced in vitro by Sclerotinia sclerotiorum consisted of numerous isoforms with pI ranging from 3.5 to 6.2. The two dominant isoforms, labelled EG1 and EG2, were purified. The pI of EG1 and EG2 were 6.2 and 3.7, respectively. Their molecular weights were, respectively, 48,000 and 34,000. EG1 and EG2 were both active towards carboxymethyl cellulose. However, EG1 was also active towards 4-methylumbelliferyl cellobioside. The amino acid compositions of EG1 and EG2 were different. The N-terminal amino acid sequences of the two enzymes showed little homology. However, the N-terminal sequence of EG1 showed considerable homology to the published N-terminal sequence of an endoglucanase (EG1) from Schizohyllum commune.

UI	MeSH Term	Description	Entries
D007526	Isoelectric Point	The pH in solutions of proteins and related compounds at which the dipolar ions are at a maximum.	Isoelectric Points,Point, Isoelectric,Points, Isoelectric
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D011489	Protein Denaturation	Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.	Denaturation, Protein,Denaturations, Protein,Protein Denaturations
D002480	Cellulase	An endocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages in CELLULOSE, lichenin, and cereal beta-glucans.	Endo-1,4-beta-Glucanase,Cellulysin,Endoglucanase,Endoglucanase A,Endoglucanase C,Endoglucanase E,Endoglucanase IV,Endoglucanase Y,beta-1,4-Glucan-4-Glucanohydrolase,Endo 1,4 beta Glucanase,beta 1,4 Glucan 4 Glucanohydrolase
D003429	Cross Reactions	Serological reactions in which an antiserum against one antigen reacts with a non-identical but closely related antigen.	Cross Reaction,Reaction, Cross,Reactions, Cross
D005110	Extracellular Space	Interstitial space between cells, occupied by INTERSTITIAL FLUID as well as amorphous and fibrous substances. For organisms with a CELL WALL, the extracellular space includes everything outside of the CELL MEMBRANE including the PERIPLASM and the cell wall.	Intercellular Space,Extracellular Spaces,Intercellular Spaces,Space, Extracellular,Space, Intercellular,Spaces, Extracellular,Spaces, Intercellular
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
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein