000 01588 a2200433 4500
005 20250516054134.0
264 0 _c20120611
008 201206s 0 0 eng d
022 _a1638-6183
024 7 _a10.1016/j.biochi.2011.08.020
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aAndjelković, Uroš
245 0 0 _aThe thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density.
_h[electronic resource]
260 _bBiochimie
_cFeb 2012
300 _a510-5 p.
_bdigital
500 _aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650 0 4 _aEnzyme Stability
650 0 4 _aGlycoproteins
_xmetabolism
650 0 4 _aGlycosylation
650 0 4 _aHot Temperature
650 0 4 _aHydrogen-Ion Concentration
650 0 4 _aIsoenzymes
_xmetabolism
650 0 4 _aMass Spectrometry
650 0 4 _aNuclear Magnetic Resonance, Biomolecular
650 0 4 _aProtein Multimerization
650 0 4 _aProtein Processing, Post-Translational
650 0 4 _aSaccharomyces cerevisiae
_xenzymology
650 0 4 _aSaccharomyces cerevisiae Proteins
_xmetabolism
650 0 4 _aStatic Electricity
650 0 4 _aThermodynamics
650 0 4 _abeta-Fructofuranosidase
_xmetabolism
700 1 _aTheisgen, Stephan
700 1 _aScheidt, Holger A
700 1 _aPetković, Marijana
700 1 _aHuster, Daniel
700 1 _aVujčić, Zoran
773 0 _tBiochimie
_gvol. 94
_gno. 2
_gp. 510-5
856 4 0 _uhttps://doi.org/10.1016/j.biochi.2011.08.020
_zAvailable from publisher's website
999 _c21146632
_d21146632