Results 151 to 160 of about 25,546 (199)

Subtilisin BPN'

open access: yesJournal of Biological Chemistry, 1965
Hiroshi Matsubara   +3 more
openaire   +2 more sources

Proteinase Inhibitors from Dog Submandibular Glands [PDF]

open access: yes, 1971
Fink, Edwin   +5 more
core  

Subtilisin NAT

open access: yesJOURNAL OF THE BREWING SOCIETY OF JAPAN, 1993
openaire   +2 more sources

Reasoning Enantioselectivity and Kinetics of Seleno-Subtilisin from the Subtilisin Template

Archives of Biochemistry and Biophysics, 1998
The 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.
Dietmar Haring, Peter Schreier
exaly   +3 more sources

Stoichiometric complexation of streptomyces subtilisin inhibitor and subtilisin

Journal of Protein Chemistry, 1991
Subtilisin (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
openaire   +2 more sources

Thermal denaturation of Streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complex

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
openaire   +2 more sources

Kinetics of subtilisin and thiolsubtilisin

Molecular and Cellular Biochemistry, 1983
Subtilisin 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
openaire   +2 more sources

The reaction of phenylmethanesulfonyl-subtilisin

Biochimica et Biophysica Acta (BBA) - Enzymology, 1972
Abstract 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
openaire   +2 more sources

Subtilisin

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
openaire   +1 more source

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