title: [Mass-spectrometric determination of specificity of proteinases].
abstract: 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.
authors.forename: M L
authors.initials: ML
authors.lastname: Aleksandrov
authors.forename: V M
authors.initials: VM
authors.lastname: Kondrat'ev
authors.forename: Iu S
authors.initials: IuS
authors.lastname: Kusner
authors.forename: O A
authors.initials: OA
authors.lastname: Mirgorodskaia
authors.forename: A V
authors.initials: AV
authors.lastname: Podtelezhnikov
mesh_terms: 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
chemical_list: D010450:Endopeptidases; C025097:Escherichia coli periplasmic proteinase; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin
vernacular_title: Mass-spektrometricheskoe opredelenie spetsifichnosti proteinaz.