3.4.21.19	analysis	increase in selectivity of immobilized metal affinity chromatography for phosphopeptides by use of enzyme for protein digestion. Enzyme cleaves proteins at acidic residues and reduces the number of acidic residues in peptides. Application of method to a selction of model proteins and to bovine milk	669617	
3.4.21.19	analysis	study of structure-function organization of anti-HIV and antitumor proteins MAP30 and GAP31 by limited proteolysis with V8-GSE, enzym may be useful for studying other proteins as well	-, 653874	
3.4.21.19	synthesis	enzyme can be used as catalyst for peptide synthesis in hydrophilic organic solvents with low water content, e.g. acetonitrile, overview	-, 653874	
3.4.21.19	synthesis	increased accumulation of recombinant enzyme in Bacillus subtilis by growth in presence of casein or gelatin. During stationary growth phase, enzyme production is stimulated by Ca2+, Mn2+, and Co2+, and inhibited by Zn2+, Fe2+, and Cu2+	670174	
3.4.21.19	synthesis	increased accumulation of recombinant enzyme in Bacillus subtilis during stationary growth phase by growth in presence of phosphate or ammonium ions, and in presence of gelatin or casein. During sporulation, enzyme production is stimulated by Ca2+, Mn2+, and Co2+, and inhibited by Zn2+, Fe2+, and Cu2+. Glucose is not inhibitory to enzyme production during stationary growth	670173	
3.4.21.19	synthesis	recombinant expression of enzyme as insoluble inclusion bodies, solubilization in 6 M guanidine-HCl in presence of reducing agent and renaturation by fast frequent dilution method. Highest yield of refolded protein at pH 8.4, 4°C. Renaturation is accompanied by gradual splitting of K12-E13 and T47-E48 bonds resulting in a 26 kDa protein that is converted to 25 kDa mature protein by limited proteolysis trypsin or subtilisin. Complete cleavage of N-terminal pro-peptide is necessary for final packing and activation of enzyme	667840	
3.4.21.19	synthesis	the enzyme could be useful for commercial preparation of casein phosphopeptides	81321