Abstract: A cysteine-free peptide is produced by producing a fused protein comprising a protein having cysteine at its N-terminal and a cysteine-free peptide ligated to the N-terminal and subsequently subjecting the fused protein to a reaction for cleaving the peptide linkage.

Abstract: A pharmaceutical composition for inhibiting cysteine protease which comprises a compound of the formula: ##STR1## wherein R.sup.1 is a hydrogen atom or an acyl group; R.sup.2, R.sup.3 and R.sup.4, same or different, are a bond, an amino acid residue or a group of the formula:--Y--R.sup.5 --in which R.sup.5 is a group resulting from imino group removal from an amino acid residue;Y is --O--, --S-- or --NR.sup.6 -- in which R.sup.6 is a hydrogen atom or a lower alkyl group;A is ##STR2## Z is a hydrogen atom, an acyl group or an optionally substituted hydrocarbon group; n is 1 or 2;provided that when n is 1, then A is ##STR3## and Y is --S-- or --NR.sup.6 --, and, at least one of R.sup.2, R.sup.3 and R.sup.4 is the formula --Y--R.sup.5 --, provided that when further all Y are --NR.sup.6 --, at least one of the amino acid residues is not bound to amhydrogen atom at the .alpha.-carbon thereof but substituted via carbon;provided that when n is 2 and Z is an aldehyde group, then R.sup.

Abstract: Disclosed is a parathyroid hormone (PTH) (1-34) derivative in which at least the amino acid residue at the 10-position is substituted by an acidic amino acid residue. The derivatives of the present invention showing potent cAMP-producing activity and bone formation activity, and thus are useful as therapeutic agents for bone diseases, etc.

Abstract: A cysteine-free peptide is produced by producing a fused protein comprising a protein having cysteine at its N-terminal and a cysteine-free peptide ligated to the N-terminal and subsequently subjecting the fused protein to a reaction for cleaving the peptide linkage.

Abstract: Disclosed are (1) a human parathyroid hormone mutein which comprises at least one modification selected from the group consisting of (i) deletion of 3 to 6 amino acid residues on the N-terminal side in the amino acid sequence of human parathyroid hormones, (ii) substitution of another lipophilic amino acid residue for at least one methionine residue in the amino acid sequence, and (iii) substitution of a cysteine residue for one amino acid residue within the region of amino acid residue Nos. 34 to 47 in the amino acid sequence; (2) a recombinant DNA having a nucleotide sequence coding for the human parathyroid hormone mutein described in (1); (3) a vector containing the recombinant DNA described in (2); (4) a vector in which the recombinant DNA described in (2) is inserted into a region controlled by an E.

Abstract: A mutein resulting from substitution of cysteins for at least one of the constitutional amino acids has a high stability, and can serve well as a pharmaceutical, such as a healing promoting agent for wounds.

Abstract: Disclosed are (1) a DNA containing a synthetic gene for expression of human parathyroid hormone represented by the following DNA sequence:TCTGTG TCCGAGATTC AGTTAATGCA TAACCTTGGC AAACATTTGA ACTCCATGGA GCGTGTAGAA TGGCTGCGTA AGAAGTTGCA GGATGTGCAC AATTTTGTTG CCTTAGGTGC CCCATTGGCT CCTCGTGATG CTGGTTCCCA AAGACCACGT AAAAAGGAAG ACAATGTCTT AGTTGAGAGC CATGAAAAAT CCCTAGGCGA GGCAGACAAG GCCGATGTGA ATGTATTAAC TAAAGCTAAA TCCCAG(2) a method for producing the DNA described in (1), which comprises enzymatically ligating a plurality of oligodeoxynucleotides to one another to form the DNA and inserting the DNA into a vector if necessary, (3) a transformant transformed by the DNA described in (1), and (4) a method for producing human parathyroid hormone which comprises cultivating the transformant described in (3), accumulating human parathyroid hormone in a culture medium, and collecting the same, whereby hPTH can be allowed to express in large amounts in a system using E. coli as a host.

Abstract: Disclosed are (A) an antibody to a peptide consisting of 8 to 9, or 12 to 14 successive amino acids from a polypeptide having nerve growth factor-like activity, (B) a method for producing the antibody, (C) a cloned hybridoma which produces the antibody, (D) a method for producing the cloned hybridoma, (E) a conjugate of the above mentioned peptide with a carrier protein, and (F) a method for purifying, and a method for detecting and assaying a polypeptide having nerve growth factor-like activity.

Abstract: Disclosed are (A) an antibody to a peptide including at least 8 successive amino acids of an amino acid sequence represented by formulaTyrAlaGluHisLysSerHisArgGlyGluTyrSerValCys AspSerGluSerLeuTrpValThrAspLysSerSerAlaIle AspIleArgGlyHisGlnValThrValLeuGlyGluIleLys ThrGlyAsnSerProValLysGlnTyrPheTyrGluThrArg CysLysGluAlaArgProValLysAsnGlyCysArgGlyIle AspAspLysHisTrpAsnSerGlnCysLysThrSerGlnThr TyrValArgAlaLeuThrSerGluAsnAsnLysLeuValGly TrpArgTrpIleArgIleAspThrSerCysValCysAlaLeu SerArgLysIleGlyArg[1],wherein said antibody has no substantial cross-reactivity with human NGF,(B) a method for producing the antibody, (C) a cloned hybridoma which produces the antibody, (D) a method for producing the cloned hybridoma, (E) a partial peptide of a polypeptide (I) including an amino acid sequence represented by formula (1), (F) a conjugate of a peptide including at least 8 successive amino acids of formula (1) with a carrier protein, (G) a method for purifying the polypeptide (I) and (H) a method for detecting and assaying t

Abstract: Parathyroid hormone (PTH) derivatives represented by the general formula: ##STR1## or a salt thereof, wherein R.sub.1 represents Ser or a D-.alpha.-amino acid residue of 4 or less carbon atoms;R.sub.2 represents a tetrapeptide chain which contains at least one water-soluble .alpha.-amino acid residue;R.sub.3 represents a tripeptide chain which contains at least one water-soluble .alpha.-amino acid residue; andR.sub.4 represents an aromatic amino acid residue or an amide thereof,except that R.sub.1 is Ser when R.sub.2 is His-Leu-Asn-Ser, R.sub.3 is E-F-Gwherein E is Arg or His, F is Lys or His, G is Lys, Leu or Gln, are disclosed.The parathyroid hormone derivatives of the present invention are stable and have high biological activity, therefore they are useful as drugs for bone diseases and the like.

Abstract: Disclosed are peptides and salts thereof represented by general formul ##STR1## wherein R.sub.1 represents Ser or Aib; R.sub.2 represents Met or a naturally occurring hydrophobic amino acid; R.sub.3 represents Leu, Ser, Lys or an aromatic amino acid; R.sub.4 represents Gly or a D-.alpha.-amino acid; R.sub.5 represents Lys or Leu; R.sub.6 represents Met or a naturally occurring hydrophobic amino acid; R.sub.7 represents Glu or a basic amino acid; R.sub.8 represents Val or basic amino acid; R.sub.9 represents Trp or 2-(1,3-dithiolane-2-yl)Trp; R.sub.10 represents Arg or His; R.sub.11 represents Lys or His; R.sub.12 represents Lys, Gln or Leu; and R.sub.13 represents Phe or Phe-NH.sub.2 ; except that simultaneously R.sub.1 consists of Ser, R.sub.2 consists of Met, R.sub.3 consists of Leu, R.sub.4 consists of Gly, D-Ala or D-Pro, R.sub.5 consists of Lys, R.sub.6 consists of Met, R.sub.7 consists of Glu, R.sub.8 consists of Val, R.sub.9 consists of Trp, R.sub.10 consists of Arg, R.sub.11 consists of Lys and R.sub.

Abstract: An indole group in an amino acid or a peptide can be protected with a group shown by the formula: ##STR1## wherein R.sub.1 and R.sub.5 each is hydrogen, methyl or methoxy; R.sub.2 and R.sub.4 each is hydrogen or methyl; and R.sub.3 is methyl or methoxy, and said group may easily be removed without affecting the amino acid or the peptide to be derived from the protected amino acid or peptide. Thus, the present invention is useful in the synthesis of a peptide containing an indole group.

Abstract: In an amino acid having .omega.-amino group protected with a protective group or a peptide having the residue of such a protected amino acid, the improvement according to which the protective group is p-methylbenzylsulfonyl group. The .omega.-amino acids protected with p-methylbenzylsulfonyl or the peptides having residues of such protected amino acids are useful for production of various peptides by liquid phase method as well as by solid-phase method, because the protective group has specific selectivity of remaining stable under the conditions commonly employed in the removal of .alpha.-aminoprotecting group but is cleaved smoothly in a good yield by hydrogen fluoride without exerting untoward unfluences upon peptides.

Abstract: The novel nonapeptide amide derivatives of the formula(Pyr)Glu-His-Trp-Ser-R.sub.1 -R.sub.2 -R.sub.3 -Arg-Pro-NH-R.sub.4wherein R.sub.1 is Tyr or Phe; R.sub.2 is D-Leu, D-Ile, D-Nle, D-Val, D-NVa, D-Abu, .alpha.-Aibu, D-Phe, D-Phg, D-Ser, D-Thr or D-Met; R.sub.3 is Leu, Ile or Nle and R.sub.4 is alkyl of 1 to 3 carbon atoms which may be substituted with hydroxyl group have a strong ovulation inducing activity.

Abstract: The novel decapeptide amide derivatives of the formula(Pyr)Glu-His-Trp-Ser-R.sub.1 -R.sub.2 -R.sub.3 -Arg-Pro-Gly-NH.sub.2wherein R.sub.1 is Tyr or Phe; R.sub.2 is D-Nle, D-Nva, D-Abu, D-Phe, D-Ser, D-Thr or D-Met and R.sub.3 is Leu, Ile or Nle have a strong ovulation inducing activity.

Abstract: A method for making N-carbobenzoxy-pGlu-His which is an important intermediate for the manufacture of several releasing hormones. The new product is made by a rapid method which produces good yields and good quality dipeptide material.