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Nematicidal Potential of <i>Purpureocillium takamizusanense</i> PMEPF27 Against Motile <i>Bursaphelenchus rainulfi</i> In Vitro. [PDF]
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Stoichiometric complexation of streptomyces subtilisin inhibitor and subtilisin
Journal of Protein Chemistry, 1991Subtilisin (Sbt) and Streptomyces subtilisin inhibitor (SSI) were analyzed either alone or together using sodium dodecylsulfate (SDS)-polyacrylamide gel electrophoresis (PAGE). With all ratios of Sbt to SSI tested, the proteins formed a stoichiometric complex, and migrated abnormally at the top of the gel.
L O, Narhi +4 more
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Biochemistry, 1981
The thermal unfolding of the microbial proteinase inhibitor Streptomyces subtilisin inhibitor (SSI) [Sato, S., & Murao, S. (1973) Agric, Biol. Chem. 37, 1067-1074), the bacterial proteinase subtilisin BPN' (EC 3.4.21.14), and the complex formed by these two proteins has been studied by differential scanning calorimetry (DSC).
K, Takahashi, J M, Sturtevant
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The thermal unfolding of the microbial proteinase inhibitor Streptomyces subtilisin inhibitor (SSI) [Sato, S., & Murao, S. (1973) Agric, Biol. Chem. 37, 1067-1074), the bacterial proteinase subtilisin BPN' (EC 3.4.21.14), and the complex formed by these two proteins has been studied by differential scanning calorimetry (DSC).
K, Takahashi, J M, Sturtevant
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Kinetics of subtilisin and thiolsubtilisin
Molecular and Cellular Biochemistry, 1983Subtilisin is a bacterial serine protease with a broad specificity in the S1 subsite. It has been very extensively studied using a variety of kinetic and physical techniques. A chemical derivative, thiolsubtilisin, has been subjected to similar studies in order to analyze the effects of the OH to SH conversion on enzyme activity.
M, Philipp, M L, Bender
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The reaction of phenylmethanesulfonyl-subtilisin
Biochimica et Biophysica Acta (BBA) - Enzymology, 1972Abstract 1. 1.|Phenylmethanesulfonyl fluoride-inactivated subtilisin is reactivated by formohydroxamic acid and hydroxylamine. Formohydroxamic acid causes reactivation to an extent of 100%. 2. 2.|From the observation that the pH-activity profile of reactivation of the inactivated subtilisin by formohydroxamic acid was S-shaped, it is ...
N, Uemitsu, M, Sugiyama, H, Matsumiya
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Reasoning Enantioselectivity and Kinetics of Seleno-Subtilisin from the Subtilisin Template
Archives of Biochemistry and Biophysics, 1998The active-site serine (Ser221) of subtilisin Carlsberg(from Bacillus licheniformis) and subtilisin BPN' (fromBacillus amyloliquefaciens) was chemically converted into a selenocystein. Contrary to subtilisin's protease activity the semisynthetic seleno-subtilisin catalyzed the reduction of hydroperoxides.
D, Häring +3 more
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1997
Abstract The complete amino acid sequence of subtilisin E was deduced from the nucleotide sequences from chromosomal DNA isolated from B. subtilis 168 (Genbank accession number K01988; Ikemura et al., 1987) and is homologous with the sequences of subtilisin BPN’ (B. amyloliquefaciens; Stahl and Ferrari, 1984; accession number X00165) and
U Shinde, M Inouye
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Abstract The complete amino acid sequence of subtilisin E was deduced from the nucleotide sequences from chromosomal DNA isolated from B. subtilis 168 (Genbank accession number K01988; Ikemura et al., 1987) and is homologous with the sequences of subtilisin BPN’ (B. amyloliquefaciens; Stahl and Ferrari, 1984; accession number X00165) and
U Shinde, M Inouye
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Photoreactivity of histidyl residues in subtilisins Novo and DY. Photooxidation of subtilisins
International Journal of Peptide and Protein Research, 1987Subtilisins Novo and DY were photoinactivated in the presence of methylene blue according to first order kinetics. The competitive inhibitor Nα‐benzoyl‐L‐arginine protected significantly against inactivation. Under the conditions employed in this study a selective photooxidation of the active site histidine 64 was achieved. Rate constants of 0.32 times
N, Genov, K, Idakieva
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Kinetic studies on the binding of Streptomyces subtilisin inhibitor with subtilisin BPN′
Archives of Biochemistry and Biophysics, 1980Abstract The binding mechanism of Streptomyces subtilisin inhibitor and subtilisin BPN′ was studied kinetically with the stopped-flow method by monitoring the protein fluorescence increase due to complex formation. In the lower concentration range of proteins, the reaction followed the second-order kinetics.
Y, Uehara, B, Tonomura, K, Hiromi
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