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- W1422914912 abstract "Publisher Summary This chapter reviews the subtilisins: the diisopropylfluorophosphate (DFP)-sensitive, extracellular, alkaline proteinaees from Bacillus subtilis and other species of Bacillus. Subtilisin BPN' has essentially the same stability characteristics as subtilisin Carlsberg. Although many of the physical properties of the subtilisins are similar, their amino acid compositions show considerable differences. Peptide mapping indicated definite similarity between subtilisin BPN' and Novo but also showed that they were different from subtilisin Carlsberg. This was substantiated by the amino acid analyses. A feature of the amino acid compositions of the subtilisins is the complete absence of cysteine or cystine in contrast to the high content of disulfide bridges in the several pancreatic proteinases. The sequence of subtilisin BPN' was deduced from studies of the tryptic, chymotryptic, peptic, and cyanogen bromide digests. The protein consists of a single polypeptide chain of 275 residues, devoid of any disulfide bridges. There is no apparent homology with the sequences of the pancreatic proteinases. The serine residue reactive with DFP is at position 221 and the sequence around that serine is different from that around the reactive serine in the mammalian pancreatic proteinases." @default.
- W1422914912 created "2016-06-24" @default.
- W1422914912 creator A5049849950 @default.
- W1422914912 creator A5054474510 @default.
- W1422914912 date "1971-01-01" @default.
- W1422914912 modified "2023-10-05" @default.
- W1422914912 title "16 Subtilisins: Primary Structure, Chemical and Physical Properties" @default.
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