Treatment of wool fibres with subtilisin and subtilisin-PEG
نویسندگان
چکیده
منابع مشابه
Subtilisin 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 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...
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 کاملAcylation of subtilisin Carlsberg by phenyl esters.
Approximate Hammett reaction constants rho calculated from k2/K8 values of several phenyl esters of N-acetyl-L-phenylalanine, hippuric acid, and beta-phenylpropionic acid are 0.0, 0.4, and 1.0 respectively. To determine whether the lack of substituent effect of k2/K8 with the N-acetyl-L-phenylalanine esters is a result of substituent-insensitive k2 or rate-limiting association of enzyme and sub...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Enzyme and Microbial Technology
سال: 2005
ISSN: 0141-0229
DOI: 10.1016/j.enzmictec.2005.01.017