title: [Solid-phase enzymatic reactions. V. Comparison of catalytic properties of subtilisin and alpha-chymotrypsin in the absence of a solvent].
abstract: Subtilisin Carlsberg (E.C. 3.4.21.14) catalyzes the hydrolysis of N-succinyl-L-phenylalanine p-nitroanilide in solid-state solvent-free hydrated protein-substrate mixtures. This process needs a certain critical degree of hydration of the protein molecule which is attained at the relative water vapour pressure (p/ps) above 0.49. The identical hydration dependency was found for the solid-state inactivation of subtilisin by phenylmethylsulphonylfluoride. Despite the fact that subtilisin and alpha-chymotrypsin belong to two different families of serine proteinases, the characteristics of their solid-state catalytic reactions are almost identical.
authors.forename: E Iu
authors.initials: EIu
authors.lastname: Maksareva
authors.forename: Iu I
authors.initials: IuI
authors.lastname: Khurgin
mesh_terms: D002384:Catalysis; D002918:Chymotrypsin / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D007124:Immunoenzyme Techniques; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D012997:Solvents; D013381:Subtilisins / Q000378:metabolism*; D014867:Water
chemical_list: D015842:Serine Proteinase Inhibitors; D012997:Solvents; D014867:Water; C011358:Suphepa; D010649:Phenylalanine; D013381:Subtilisins; D002918:Chymotrypsin