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Dissociation constants and thermal stability of complexes of Bacillus intermedius RNase and the protein inhibitor of Bacillus amyloliquefaciens RNase
Author(s) -
Yakovlev G.I.,
Moiseyev G.P.,
Protasevich I.I.,
Ranjbar B.,
Bocharov A.L.,
Kirpichnikov M.P.,
Gilli R.M.,
Briand C.M.,
Hartley R.W.,
Makarov A.A.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00491-q
Subject(s) - barnase , bacillus amyloliquefaciens , rnase p , chemistry , ribonuclease , dissociation constant , denaturation (fissile materials) , biochemistry , biophysics , stereochemistry , biology , rna , receptor , nuclear chemistry , fermentation , gene
Binase, the extracellular ribonuclease of Bacillus intermedius , is inhibited by barstar, the natural protein inhibitor of the homologous RNase, barnase, of B. intermedius . The dissociation constants of the binase complexes with barstar and its double Cys 40.82 Ala mutant are about 10 −12 M, only 5 to 43 times higher than those of the barnase‐barstar complex. As with barnase, the denaturation temperature of binase is raised dramatically in the complex. Calorimetric studies of the formation and stability of the binase‐barstar complex show that the binase reaction with barstar is qualitatively similar to that of barnase but some significant quantitative differences are reported.