Kinetic patterns of glucoamylase isozymes isolated from Aspergillus species
| Autor: | D. E. Hensley, M.J. Smiley, Helen J. Gasdorf, Karl L. Smiley |
|---|---|
| Rok vydání: | 1971 |
| Předmět: |
Glycoside Hydrolases
Starch Biophysics Oligosaccharides Biology Polysaccharide Biochemistry Michaelis–Menten kinetics Isozyme Chromatography DEAE-Cellulose chemistry.chemical_compound Drug Stability Polysaccharides Glycoside hydrolase Maltose Molecular Biology chemistry.chemical_classification Autoanalysis Glycogen Hydrogen-Ion Concentration Isoenzymes Molecular Weight Electrophoresis Kinetics Aspergillus chemistry Chromatography Gel |
| Zdroj: | Archives of biochemistry and biophysics. 144(2) |
| ISSN: | 0003-9861 |
| Popis: | The existence of multiple forms of glucoamylase has been known for some time. However, little information is available to differentiate these isozymes other than their electrophoretic mobility. It has now been found that the two forms of glucoamylase from several different Aspergillus strains do differ in their rate of attack on starch and glycogen. The Michaelis constant of the least charged isozyme on glycogen approaches infinity, whereas on starch it is several times greater than the more charged form. On small oligosaccharides and maltose the two forms show the same K m and V max values. In addition to kinetic differences, the two isozyme forms differ in their molecular weight. |
| Databáze: | OpenAIRE |
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