The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density.

Andjelković, Uroš

The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density. [electronic resource] - Biochimie Feb 2012 - 510-5 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

1638-6183

10.1016/j.biochi.2011.08.020 doi


Enzyme Stability
Glycoproteins--metabolism
Glycosylation
Hot Temperature
Hydrogen-Ion Concentration
Isoenzymes--metabolism
Mass Spectrometry
Nuclear Magnetic Resonance, Biomolecular
Protein Multimerization
Protein Processing, Post-Translational
Saccharomyces cerevisiae--enzymology
Saccharomyces cerevisiae Proteins--metabolism
Static Electricity
Thermodynamics
beta-Fructofuranosidase--metabolism