منابع مشابه
Subtilisin Amylosacchariticus. II. Isolation and sequence of the tryptic and cyanogen bromide peptides.
Previous work on the primary structures of subtilisins BPN’ (1, 2), Novo (3), and Carlsberg (4) had shown that tryptic digestion and resolution of the resulting peptides by either ion exchange chromatography or gel filtration served as a useful first step in determining the amino acid sequences of these proteins. Accordingly, the diisopropylphosphoryl derivative of subtilisin Amylosacchariticus...
متن کاملSubtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships.
Evidence is presented for the complete amino acid sequence of subtilisin Carlsberg. The protein consists of a single peptide chain of 274 residues. Comparison with subtilisin BPN’ shows 84 amino acid differences and 1 additional residue in BPN’. The 84 differences can be accounted for on the basis of single or double nucleotide replacements. Within the subtilisins, there are a number of distinc...
متن کاملSubtilisin modification of monodeamidated ribonuclease-A.
Limited proteolysis of RNAase-Aa(1) (monodeamidated ribonuclease-A) by subtilisin results in the formation of an active RNAase-S type of derivative, namely RNAase-Aa(1)S. RNAase-Aa(1)S was chromatographically distinct from RNAase-S, but exhibited very nearly the same enzymic activity, antigenic conformation and susceptibility to trypsin as did RNAase-S. Fractionation of RNAase-Aa(1)S by trichlo...
متن کاملDye-sensitized photooxidation of neutral protease from Bacillus subtilis var. amylosacchariticus: assignment of histidine residue oxidized.
The neutral protease of Bacillus subtilis var. amylosacchariticus was photooxidized in the presence of methylene blue, by which treatment the enzyme was rapidly inactivated. The inactive enzyme was digested with endoproteinase Asp-N, the resultant peptides were separated by HPLC, and their amino acid sequences were compared with those obtained from the unmodified enzyme. Of four peptides that c...
متن کاملSpecificities of &hymotrypsin and Subtilisin Carl&erg
A study of the comparative specificities of cr-chymotrypsin and subtilisin Carlsberg has been focused mainly on the extent to which a-acetamido groups of some specific and nonspecific activated ester substrates affect the reactivity of each enzyme. Comparisons are based upon k, and k,: K,,, corrected for substrate intrinsic reactivities ((k,), and (k,: K&J. Among p-nitrophenyl P-phenylpropionat...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)81146-6