[Mass-spectrometric determination of specificity of proteinases].
Analysis of methods of the proteinase substrate specificity determination revealed that Michaelis constants found from the rates of hydrolysis of small synthetic substrates cannot be a good measure of selectivity, especially for proteinases of broad specificity used for hydrolysis of substrates of high molecular mass with multiple cleavage sites. Mass-spectrometric studies (ERIAD) of the hydrolysis of the insulin B chain with trypsin, chymotrypsin, and proteinase I showed that monitoring of the reaction mixtures by means of this technique gives more reliable information on the selectivity of proteinase towards high-molecular substrates.
Aleksandrov
M L
ML
Kondrat'ev
V M
VM
Kusner
Iu S
IuS
Mirgorodskaia
O A
OA
Podtelezhnikov
A V
AV
D002918:Chymotrypsin / Q000032:analysis; D010450:Endopeptidases / Q000032:analysis*; D006868:Hydrolysis; D013058:Mass Spectrometry; D012697:Serine Endopeptidases / Q000032:analysis; D013379:Substrate Specificity; D014357:Trypsin / Q000032:analysis
D010450:Endopeptidases; C025097:Escherichia coli periplasmic proteinase; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin
Mass-spektrometricheskoe opredelenie spetsifichnosti proteinaz.