Temperature dependent pH-instability of some alpha-L-arabinofuranosidases.
In this paper are described alpha-L-arabinofuranosidases, partially purified from some moulds, with very high lability of their activity to weakly alkaline or neutral pH-values. This pH-lability strongly depends on temperature. The form of the inactivation curves suggests involvement of charge changes in this irreversible process. These enzymes may be useful for optimization of the tumor therapy concept described by Graffi (5).
Butschak
G
G
Central Institute of Molecular Biology, Academy of Sciences of the GDR, Berlin-Buch.
Küster
A
A
Schulze
B
B
Graffi
A
A
D001203:Ascomycota / Q000201:enzymology; D004355:Drug Stability; D005670:Fusarium / Q000201:enzymology; D006026:Glycoside Hydrolases / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D013696:Temperature
D006026:Glycoside Hydrolases; C019713:alpha-N-arabinofuranosidase