Abstract: According to the present invention, a novel protease derived from Streptomyces fradiae for cleaving the C-terminal of a glutamic acid residue in an amino acid sequence of a polypeptide and a production method for this protease from Streptomyces fradiae are provided, and the characteristics of this protease are made clear. Further, DNA sequences for encoding this protease and a prepropeptide are also made clear. The protease specific to glutamic acid can be used for a variety of purposes including analysis of a protein and cleavage of a peptide chain at a desired site in a fusion protein.

Abstract: A novel protease derived from Bacillus licheniformis is provided. The protease cleaves the peptide bonds at the carboxyl termini of glutamic acid residues in polypeptides. The protease contains an amino acid sequence from serine in the +1 position to glutamine in the +222 position of SEQ ID NO: 1.

Abstract: DNA sequences encoding modified varieties of human PSTI possessing excellent stability in terms of decreased susceptibility to decomposition by proteolytic enzymes such as trypsin, as compared with natural human PSTI, as well as the modified varieties of human PSTI obtained by the expression of the DNA sequences.

Abstract: The whole DNA sequence coding for flagellin of E. coli (hag gene) cloned in phage .lambda. was determined. The hag gene is introduced into pBR322 and the region of the hag gene concerning the antigencity of flagella is lacked, into which linkers are inserted. Where the vector in which foreign DNA is inserted in the linker is introduced in E. coli forming no flagella, the E. coli can form flagella and possesses motility. The flagella comprises flagellin fused with foreign peptide encoded by the foreign DNA. Namely, the foreign peptide is excreted outside of bacteria. This system can be utilized in determination of epitope and preparation of antigen as well as excretion of peptide.

Abstract: A polypeptide of the formula:X.sub.1 --Tyr--Ser--X.sub.2 --X.sub.3 --His--Phe--Arg--Trp--Gly--Lys--Pro--Val--Gly--(Lys).sub.n --Ywherein X.sub.1 is .alpha.-aminoisobutyric acid, .beta.-alanine, L-serine, D-serine, glycine, D-alanine, .gamma.-aminobutyric acid or sarcosine residue; X.sub.2 is L-methionine, L-norleucine, L-isoleucine or L-norvaline residue; X.sub.3 is L-glutamic acid or L-glutamine residue; n is an integer of 5-10; and Y is --R.sub.1, ##STR1## wherein R.sub.1 is hydroxy or lower alkoxy having 1-5 carbon atoms; R.sub.2, R.sub.3, R.sub.4 and R.sub.5 are each hydrogen or lower alkyl having 1-5 carbon atoms; m is an integer of 1-10 and Y is a group bound to the carbonyl group of the C-terminal lysine residue; non-toxic acid addition salts thereof; and complexes thereof; being useful as a medicament owing to their strong adrenal-stimulating activity with protracted action and little side effects.

Abstract: A polypeptide of the formula:X.sub.1 -Tyr-Ser-X.sub.2 -X.sub.3 -His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-(Lys).sub.n -Ywherein X.sub.1 is .alpha.-aminoisobutyric acid, .beta.-alanine, L-serine, glycine, D-serine, D-alanine, .gamma.-aminobutyric acid or sarcosine residue; X.sub.2 is L-methionine, L-norleucine, L-isoleucine or L-norvaline residue; X.sub.3 is L-glutamic acid or L-glutamine residue; n is an integer of 1-4 and Y is a group of ##STR1## which is linked to the carbonyl group of the C-terminal lysine residue, wherein R.sub.1 and R.sub.2 are each hydrogen or the same or different lower alkyl having 1-5 carbon atoms, and R.sub.1 and R.sub.2, when taken together with or without another hetero atom, form a substituted or unsubstituted nitrogen containing heterocyclic ring, with the proviso that a peptide when X.sub.1 is a .alpha.-aminoisobutyric acid or D-serine, R.sub.1 and R.sub.