Abstract: A method of treating erectile dysfunctions in mammals and men, by administering to the mammal or man a pharmaceutical composition comprising a therapeutically effective amount of a calcitonin gene-related peptide.

Abstract: Novel polypeptide derivatives, acid-addition salts thereof and complexes thereof, having the activities for inhibiting bone calcium absorption, for lowering the blood level of calcium, as analgesics, for inhibiting secretion of the gastric juice.Pharmaceutical composition can be prepared by formulating, at least one of the novel polypeptide derivatives, acid-addition salts thereof and complexes thereof, together with a proteolytic enzyme inhibitors and/or pharmaceutically acceptable acids.The pharmaceutical composition are quite effective as agents for curing hypercalcemia, for curing Peget's disease, for curing osteoporosis, analgetic agent, anti-ulcerative agent and the like.

Abstract: Synthetic hypocalcemic peptides which are similar in biological properties to native calcitonins as clinically useful agents. The peptides comprise analogues of native calcitonins having amino acid substitutions and deletions which act to improve potency, prolong duration of the hormonal effect, enhance receptor binding, and increase oral or nasal bioavailability. The calcitonin peptide analogues are less expensive and more easily synthesized than native calcitonins, and have improved resistance to inactivation or degradation. Methods are provided for the synthesis of these peptides.Also, disclosed are novel cyclic peptides, including calcitonin, having increased stability with respect to proteolysis. Methods for the synthesis of these peptides are provided, comprising converting disulfide cyclic peptides and proteins to enzymatically and chemically stable cyclic peptide structures by the replacement of cysteine residues with dicarboxylic acids and diamino acids.

Abstract: Covalently-linked complexes (CLCs) for targeting a defined population of cells, comprising a targeting protein; a cytotoxic agent; and an enhancing moiety, wherein the enhancing moiety is capable of promoting CLC-target cell interaction are disclosed. Methods for using the claimed CLCs to obtain enhanced in vivo cytotoxicity and enhanced in vivo imaging are also described.

Abstract: Novel synthetic polypeptide derivatives, i.e., novel calcitonin derivatives, having improved basic physiological activities of the corresponding natural calcitonins, i.e., the activity for lowering the blood level of calcium, the activity as an analgesic, as well as the activity for inhibiting the secretion of the gastric juice. Thus these synthetic calcitonins are effective as agents for curing hypercalcemia, analgetic agents, anti-ulcerative agents and the like.

Abstract: Calcitonin derivatives wherein at least one of the first cysteine residue and the seventh cysteine residue is S-sulfonated; processes for the production of the calcitonin derivatives comprising the steps of reacting a calcitonin with a sulfite anion or both a sulfite anion and an oxidizing agent to form the S-sulfonated derivative, and recovering the sulfonated calcitonin derivative; a pharmaceutical composition comprising the S-sulfonated calcitonin derivative; and a method of treating a patient having a disease wherein a decrease of a serum calcium level is desired, by administering the S-sulfonated calcitonin derivative to the patient.

Abstract: Peptide analogues of human humoral hypercalcemic factor (hHCF) that contain a lactam bridge act as inhibitors of the naturally occurring peptide. A lactam bridge between Lys and Asp situated five residues (inclusive) apart confers rigidity to that region of the peptide, and enhances the helical nature and metabolic stability of the peptide analogue.

Abstract: Compositions comprising a calcitonin gene related peptide and, as an absorption enhancer, a glycyrrhizinate.

Abstract: A compound of the formula ##STR1## wherein Y is sulfur or methylene and A is Asn or Asp, or a pharmaceutically acceptable salt thereof is useful for the treatment of calcium metabolic disorders, cardiac disease and ulcers, and for the improvement of cranial circulation.

Abstract: Disclosed are intranasal formulations comprising calcitonin and .sup..DELTA. -aminolevulinic acid in a pharmaceutically acceptable excipient.

Abstract: There is disclosed a calcitonin derivative and its salt, comprising an amino acid residue at the 1-position of calcitonin which is a cyclic amino acid residue represented by the formula: ##STR1## wherein X represents a sulfur atom or a methylene group; and n represents an integer of 0 or 1. and an amino acid residue at the 7-position which is a cysteine residue which may be substituted with an appropriate protective group.

Abstract: Disclosed are rectal and vaginal suppository formulations comprising calcitonin and caprylic acid monoglyceride in a pharmaceutically acceptable suppository vehicle.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have a histidine in position 17. The position 17 histidine is omitted. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: A compound of the formula ##STR1## wherein R is H or H-Ala-NH- and when A is Asp, B is Asp or Glu, C is Leu and D is Val; when A is Asn and B is Gly, C is Phe and D is Gly; when A is Asn, B is Asp or Glu and C is Leu, D is Gly; and when A is Asn, B is Asp or Glu, and C is Phe, D is Val, or a pharmaceutically acceptable salt thereof, is useful for the treatment of calcium metabolic disorders, cardiac disease and ulcers, and for the improvement of cerebral circulation.

Abstract: The invention relates to a substance from the calcitonin group, which substance can be isolated from the human body or can be obtained in a different manner, but clearly differs from the known human calcitonin-(1-32), the said substance having hypocalcaemic activity.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which have an alanine in position 19 instead of the natural leucine or phenylalanine found in those positions. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: A complex of a therapeutic agent is disclosed in which the therapeutic agent is complexed to an ammonium ion selected from the group consisting of ##STR1## where R.sup.1 and R.sup.2 are the same or different and are alkyl or hydroxy substituted alkyl containing 1 to 6 carbon atoms; andR, R' and R" are the same or different and are saturated or unsaturated aliphatics containing at least 10 carbon atoms, ##STR2## where R.sup.1, R.sup.2 and R" are as defined above, ##STR3## where R.sup.3 is independently alkyl or hydroxy substituted alkyl containing at least 10 carbon atoms; and R.sup.1, R.sup.2, R.sup.3 and R' having the meanings given above; and ##STR4## where R.sup.1, R.sup.2 and R.sup.3 have the meanings given above. The therapeutic agent is heparin, a biologically active peptide or protein or an antineoplastic drug. The therapeutic agent may also be covalently bonded to a triglyceride type backbone to form a compound.

Abstract: New hypocalcaemic peptides are disclosed of the formula ##STR1## wherein X represents H for the replacement of the N alpha amino group or acyl groups for the acylation of the N alpha amino group, the N-alpha amino group. The acyl groups are carboxylic acids especially formic, acetic, propionic, buteric, valeric, hexanoic, heptanoic, octanoic, and nonanoic acids or their respective isomers, L-lactic acid and the half amides of malonic, succinic, glutaric and adipic acids. Y is L-valine, glycine, L-methionine, L-alanine, L-leucine or L-isoleucine.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which are amide analogs of natural calcitonins.

Abstract: A highly sensitive, immunoassay method for determining the amount of an analyte in a sample containing a known analyte in an unknown concentration is provided. Sample; a polypeptide-labeled analog of the analyte, an antibody specific for said analyte, a polypeptide partner capable of non-covalently binding with the polypeptide-labeled analyte to form a complex having catalytic activity, and a substrate capable of being converted to a reporter molecule by the catalytic activity of said complex are brought together in a medium. The polypeptide-labeled analyte analog is capable of competitively binding to the antibody and the polypeptide partner, the antibody inhibiting the formation of a catalytically active complex in the absence of analyte, and the concentration of the antibody, polypeptide partner and polypeptide-labeled analyte are such as to cause varying amounts of analyte to be directly related to the conversion of the substrate to the reporter molecule.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have a leucine in position 19, a glutamine in position 20, or a threonine in position 21. All three amino acids are omitted. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: New hypocalcaemic peptides are disclosed of the formula ##STR1## wherein X represents acyl groups for the acylation of the N alpha-amino group and the radicals of carboxylic acids especially of formic, acetic, propionic, buteric, valeric, hexanoic, heptanoic, octanoic, and nonanoic acids along with all their respective isomers. We also wish to include L-lactic acid along with the half amides of malonic, succinic, glutaric and adipic acids.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have a leucine in position 19, a glutamine in position 20, a threonine in position 21, and a tyrosine in position 22. All four amino acids are omitted. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: A compound of formula I ##STR1## wherein R is H or R'CO wherein R'CO is an acyl radical of a carboxylic acid,Y.sub.1 is the radical linked to an alpha carbon atom an .alpha.-amino acid,Y.sub.2 is the radical linked to an alpha carbon atom of an .alpha.-amino acid, ##STR2## --CH.sub.2 --S--S--CH.sub.2 --CH.sub.2 --COOH, --(CH.sub.2).sub.p --COOH or --CH.sub.2 --S--Y.sub.3,Y.sub.3 is (C.sub.1-4)alkyl or benzyl optionally substituted by methyl or methoxy,or CH.sub.3 CO--NH--CH.sub.2 --,n is 1 to 4,A.sub.6 is Thr or D-Thr,p is 3 to 5,A.sub.8 is the aminoacyl radical of a neutral, lipophilic L-.alpha.-aminoacid,A.sub.9 is the aminoacyl radical of a neutral, lipophilic L- or D-.alpha.-aminoacid,Z is a polypeptide radical corresponding to the polypeptide radical in positions 10 to 31 of a natural calcitonin or a derivative or analogue thereof having a hypocalcemic effect,wherein, when there is more than one Y.sub.1 radical, these are the same or different, and with the exception of radical A.sub.

Abstract: New peptides are disclosed which have biological activity of the same type as the known calcitonins and which have a glycine at position 8 instead of the natural valine found in that position. In addition these new peptides do not have a leucine in position 19. The position 19 leucine is omitted. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: A peptide represented by the following formula: ##STR1## wherein Y means a sulfur atom or methylene group, A stands for Asp or Asn, B denotes Val or Met and C is Asn or Ser, or a salt thereof.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have a leucine in position 19 or a glutamine in position 20. Both amino acids are omitted. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: Described are peptides that have, as partial sequence of a larger peptide, or exclusively, the amino acid sequence of the formula I ##STR1## in which the cysteine residues can form intra- or inter-molecular disulphide bridges, and derivatives thereof having an amidated terminal carboxy group and/or an acylated terminal amino group, and their salts, DNA sequences that code for the mentioned peptides, micro-organisms that contain these DNA sequences, processes for the manufacture thereof, pharmaceutical preparations that contain the mentioned peptides in the form of their amides, and the use of these peptide-amides for the treatment of coronary circulation disorders and bone metabolism disorders.

Abstract: A peptide with C-terminal proline amide is produced by reacting in aqueous solution a protein substrate having C-terminal prolyl-leucine, prolyl-isoleucine, prolyl-valine, or prolyl-phenylalanine with carboxypeptidase Y in the presence of ammonia. The ammonia is preferably generated by the aqueous reaction of an ammonium salt and an alkali. An example of the peptide product is human calcitonin.

Abstract: There are disclosed a novel polypeptide represented by the formula shown below or its acid addition salt or complex: ##STR1## wherein Ala represents alanine, Ser serine, Leu leucine, Thr threonine, Val valine, Gly glycine, Lys lysine, Gln glutamine, Glu glutamic acid, His histidine, Tyr tyrosine, Pro proline, Arg arginine, Asp aspartic acid, and n represents an integer of 3 to 7,and a process for producing the same comprising forming a peptide or polypeptide represented by the above formula and subjecting the structural units containing a peptide residue represented by the formula: ##STR2## wherein R represents an active ester residue, Ala, Ser, Leu, Thr and n have the same meanings as defined above,formed in any step of the reaction to cyclization reaction.

Abstract: Compounds of the formula: ##STR1## wherein R.sub.1 is a moiety selected from the group consisting of ##STR2## R.sub.2 -R.sub.22 are amino acid moieties wherein R.sub.2 is an optional moiety which when present is selected from the group consisting of Ser and Gly,R.sub.8 is Leu or Val,R.sub.10 is Gln, Lys, or Gly,R.sub.11, R.sub.14, and R.sub.20 are each independently selected from the group consisting of Gln and Lys,R.sub.12 is Leu or Trp,R.sub.13 is Gln or Ser,R.sub.17 is Gln or His,R.sub.19 is Leu or Cys,R.sub.21 is Gln or Thr,R.sub.22 is an optional moiety which when present is selected from the group consisting of Leu and Tyr;R.sub.24 -R.sub.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have a disulfide bond connecting the cysteines at positions one and seven. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin partially protected peptides.

Abstract: New peptides are disclosed which have biological activity of the same type as calcitonins and which have been modified with desaminocysteine and .alpha.-aminosuberic acid at the N-terminal and new amino acid substituents at the penultimate position of the C-terminal.

Abstract: New calcitonin analogs are disclosed which have biological activity of the same type as known calcitonins and which have a D-amino acid substituent in at least one of the positions 31 and 32 instead of the natural L-amino acid units. The calcitonin analog may be analogs of salmon, eel, chicken, bovine, porcine, ovine, murine or human calcitonins.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which are amide analogs of natural calcitonins.

Abstract: New polypeptides are disclosed which have biological activity of the same degree as known calcitonins and which have amino acid substituents in position 31 instead of the naturally occuring amino acids--Thr, Ala, Val.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which have an alanine in positions 16 and 19 instead of the natural leucine or phenylalanine found in those positions. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have a leucine in position 19. The position 19 leucine is omitted. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which have an S-acetamidomethyl cysteine at one and an alanine at seven, or an alanine at one and an S-acetamidomethyl cysteine at seven. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin-type peptides.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins; which have a serine in position 6 while the position 19 leucine is omitted. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: Peptides, such as calcitonin, having two cysteine residues connected by a disulfide bond are prepared by a process which includes the step of cyclizing the cysteines at a pH of 8.5 to 9.0, and a concentration of 0.4 to 1.8 mg of peptide per ml of solution. These novel conditions produce rapid cyclization with an unforeseen improvement in yield.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which have an methionine in position 8 instead of the natural valine found in that position. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have a serine in position 2 nor an asparagine in position 3. Both serine 2 and asparagine 3 are omitted. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have cysteines at positions one and seven. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin-type peptides.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and do not have an amino group on cysteine one and also are substitution analogs of the natural calcitonins. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: New peptides ae disclosed which have biological activity of the same type as known calcitonins and contains only twenty-three amino acids rather than the normally occurring thirty-two amino acids. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have a leucine in position 4. The position 4 leucine is omitted. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have a serine in position 13. The position 13 serine is omitted. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which have a shorter amino acid chain than natural calcitonins and are also substitution analogs of the natural calcitonins. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin peptides.

Abstract: Human calcitonin in the form of four components and process for their isolation from C-cells material.