4.2.1.30	additional information	-	-	33824	
4.2.1.30	additional information	-	studies on the thermal dissociation of the enzyme	33820	
4.2.1.30	30	-	30 min, potassium phosphate buffer, pH 8.6, apoenzyme is quite stable. On addition of coenzyme B12 to the incubation mixture the holoenzyme is formed	33823	
4.2.1.30	45	-	activity is lost dramatically at temperatures above 45°C	725951	
4.2.1.30	45	-	t1/2: 1 h	704770	
4.2.1.30	46	-	4 min, 50% destruction of the apoenzyme	33824	
4.2.1.30	50	-	subunit A: quickly inactivated at temperatures above, K+ and Na+ stabilize at high concentrations	33820	
4.2.1.30	60	-	dissociation of the inactive enzyme complex with hydroxocobalamin, if the enzyme complex is heated to over 60°C. Heating products: an active subunit B, an inactive subunit A, and a B12 derivative. K+ inhibit heat-mediated dissociation	33820	
4.2.1.30	70	-	inactivation of subunit A at 70°C is reversible	33824	
4.2.1.30	70	-	inactive enzyme complex with hydroxocobalamin: quite stable	33819	
4.2.1.30	75	-	subunit B is stabilized by K+, Na2HPO4 and K2HPO4 protect against thermal inactivation	33820	
4.2.1.30	78	-	K+ stabilizes inactive enzyme complex with hydroxocobalamin	33819	
4.2.1.30	83	-	3 min, 0.6 M KCl, inactive enzyme complex with hydroxocobalamin loses 50% of activity, K+ and Rb+ have the greatest heat-stabilizing effect	33820