Abstract: The present invention relates to a compound which is highly selective for CRFR1 without having any significant cross-reactivity for corticotropin-releasing-factor-receptor-2 (CRFR2) and/or corticotropin-releasing-factor-binding protein (CRFBP), said compound comprising or alternatively consisting of the amino acid sequence as depicted in SEQ ID No: 1. In another aspect, the present invention relates to a pharmaceutical and/or diagnostic composition comprising the novel CRFR1 agonist of the present invention. The present invention also provides a kit comprising the novel CRFR1 agonist of the present invention and optionally instructions to use.

Abstract: The present invention relates to an antagonist of the ligand of the Corticotropin-Releasing Factor Receptor, type 2 (CRFR2) lacking the 8 to 10 N-terminal amino acids of native sauvagine. The present invention also relates to an antagonist of the ligand of the Corticotropin-Releasing Factor Receptor, type 2 (CRFR2) lacking the 11 N-terminal amino acids of native sauvagine, wherein the N-terminal amino acid of said antagonist is a charged amino acid. Furthermore, the present invention relates to a polynucleotide encoding the antagonist of the present invention, a vector comprising the polynucleotide of the present invention, and a host comprising the polynucleotide or the vector of the present invention. Also described are a method for producing the antagonist of the present invention, antibodies directed the antagonist of the present invention, as well as anti-idiotypic antibodies directed against the antibody of the present invention.

Abstract: The present invention relates to a ligand of the Corticotropin-Releasing Factor (CRF)-binding protein (CRFBP) selected from the group consisting of CRF, Urocortin (Ucn), and Urotensin, said ligand comprising a covalently linked benzophenone moiety. Further, the present invention relates to a process for the purification of a CRFBP which comprises reacting said CRFBP with the ligand of the invention, performing photoaffinity labeling, and purifying the resultant photoreaction products by HPLC. The present invention also relates to the use of the ligand of the invention for detecting CRFBP and for identifying the binding site within CRFBP. The present invention also relates to a method for identifying an inhibitor of the binding of ARF to CRFBP.

Abstract: The present invention relates to a method for improving the antagonistic/agonistic properties of peptidic antagonists/agonists of the corticotropin-releasing factor receptor (CRFR). Further, the present invention relates to an antagonist of the ligand of the corticotropin-releasing factor receptor (CRFR) comprising or alternatively consisting of the amino acid sequence of astressin wherein at least Ala at position 11 is replaced by another amino acid. Further, the present invention relates to an antibody directed against the agonist or antagonist of the present invention. Also described is an anti-idiotypic antibody which is directed against the antibody(ies) of the invention. The present invention also relates to a pharmaceutical or diagnostic composition comprising the antagonist, the agonist, the antibody(ies) and/or the anti-idiotypic antibody of the invention.

Abstract: A dimeric protein with inhibin activity is isolated from ram reta testis fluid using reverse-phase high-performance liquid chromatography and gel filtration. The isolated molecule is composed of two chains having apparent molecular weights of about 18,000 and about 16,500 to 14,500 Daltons, as measured by gel electrophoresis, which are bound together by disulfide bonding and the longer of which is likely glycosylated. Microsequencing revealed the NH.sub.2 -terminal portion of the longer chain to be Ser- Thr-Pro-Pro-Leu-Pro-Trp-Pro-Trp-Ser-Pro-Ala-Ala-Leu-Arg-Leu-Gln-Arg-Pro-Pr o- Glu-Glu-Pro-Ala-Ala-His-Ala-Asp-Cys and of the shorther chain to by Gly-Leu-Glu-Cys-Asp-Gly-Lys-Val-Asn-Ile-Cys-Cys-Lys-Lys-Gln-Phe. This dimeric protein specifically inhibits basal secretion of FSH, but not of LH, in a rat anterior pituitary monolayer culture system, exhibiting a half-maximal effective dose of about 0.1 to 0.3 ng/ml.

Abstract: A 28,000-dalton protein with FSH-releasing activity is isolated from porcine follicular fluid in a multi-step procedure including gel filtration, ion exchange chromatography and several reverse-phase high-performance liquid chromatography steps. The 28 kD protein promotes secretion of FSH, but not of LH, in a rat anterior pituitary monolayer culture system, exhibiting an EC.sub.50 of 0.5 ng/ml. These peptides are dimers of inhibin .beta.-chains of mammals, and homodimers or heterodimers of the .beta..sub.A and .beta..sub.B chains are biologically active to regulate fertility of various mammalian species, including humans.

Abstract: A 32,000-Dalton protein with inhibin activity is isolated from porcine follicular fluid which is composed of two chains having molecular weights of about 18,000 and about 14,000 Daltons, which are bound together by disulfide bonding. Microsequencing revealed the NH.sub.2 -terminal portion of the 18 kD chain to be Ser-Thr-Ala-Pro-Leu-Pro-Trp-Pro-Trp-Ser-Pro-Ala-Ala-Leu-Arg-Leu-Leu-Gln-Ar g- Pro-Pro-Glu-Glu-Pro-Ala-Val and of the 14 kD chain to be Gly-Leu-Glu-Cys with the next 21 residues believed to be Asp-Gly-Ser-His-Asn-Leu-Asp-Ser-Arg-Gln-Gln-Phe-Phe-Ile-Asp-Phe-Arg-Leu-Il e-G y-Trp. This 32 kD protein specifically inhibits basal secretion of FSH, but not of LH. Antibodies raised against a synthetic replicate of the N-terminal six residues of the 18 kD chain are effective to reduce the activity of highly purified 32 kD inhibin and may be administered to mammalian animals for the purpose of neutralizing endogenous inhibin and thereby increasing gonadotropin secretion.

Abstract: The invention provides peptides which are particularly potent in stimulating the release of pituitary GH in fish and amphibians and which have a substantial portion or all of the following sequence: His-Ala-Asp-Gly-R.sub.5 -Phe-Asn-Lys-Ala-Tyr-Arg-Lys-Ala-Leu-Gly-Gln-Leu- Ser-Ala-Arg-Lys-Tyr-Leu-His-Thr-Leu-R.sub.27 -R.sub.28 -R.sub.29 -R.sub.30 -R.sub.31 -Gly-R.sub.33 -R.sub.34 -R.sub.35 -R.sub.36 -R.sub.37 - R.sub.38 -R.sub.39 -R.sub.40 -R.sub.41 -R.sub.42 -R.sub.43 -R.sub.44 -Ser wherein R.sub.5 is Met, Leu, Val, Nva, Gln, Thr, Ile or Nle; R.sub.27 is Met, Leu, Val, Nva, Gln, Thr, Ile or Nle; R.sub.28 is Ala, Ser or Asn; R.sub.29 is Lys or Arg; R.sub.30 is Arg or Gln; R.sub.31 is Val or Gln; R.sub.33 is Gly or Glu; R.sub.34 is Gly, Arg or Ser; R.sub.35 is Ser or Asn; R.sub.36 is Met, Leu, Val, Nva, Gln, Thr, Ile or Nle; R.sub.37 is Ile or Glu; R.sub.38 is Glu, Gln or Arg; R.sub.39 is Asp, Arg or Gly; R.sub.40 is Asp, Ser or Ala; R.sub.41 is Asn, Arg or Lys; R.sub.42 is Glu, Phe, Ala or Val; R.sub.

Abstract: Anglerfish somatostatin-28 has the formula: ##STR1## Anglerfish somatostation-28 is insulin-selective when administered in vivo and is useful for the treatment of insulinoma. The 14-residue C-terminal peptide may also be used.

Abstract: Proteins with inhibin activity having a weight of about 32,000 daltons. The molecule is composed of two chains having molecular weights of about 18,000 and about 14,000 daltons, respectively, which are bound together by disulfide bonding. The 18K chain is obtained from the human inhibin gene and has the formula: H-Ser-Thr-Pro-Leu-Met-Ser-Trp-Pro-Trp-Ser-Pro-Ser-Ala-Leu-Arg-Leu-Leu-Gln- Arg-Pro-Pro-Glu-Glu-Pro-Ala-Ala-His-Ala-Asn-Cys-His-Arg-Val-Ala-Leu-Asn-Ile -Ser-Phe-Gln-Glu-Leu-Gly-Trp-Glu-Arg-Trp-Ile-Val-Tyr-Pro-Pro-Ser-Phe-R.sub. 65 -Phe-His-Tyr-Cys-His-Gly-Gly-Cys-Gly-Leu-His-Ile-Pro-Pro-Asn-Leu-Ser-Leu-P ro-Val-Pro-Gly-Ala-Pro-Pro-Thr-Pro-Ala-Gln-Pro-Tyr-Ser-Leu-Leu-Pro-Gly-Ala- Gln-Pro-Cys-Cys-Ala-Ala-Leu-Pro-Gly-Thr-Met-Arg-Pro-Leu-His-Val-Arg-Thr-Thr -Ser-Asp-Gly-Gly-Tyr-Ser-P e-Lys-Tyr-Glu-Thr-Val-Pro-Asn-Leu-Leu-Thr-Gln-His-Cys-Ala-Cys-Ile-OH, wherein R.sub.65 is Ile or Arg. The 18K chain is connected by disulfide bonding to the 14K chain.

Abstract: A bag-filling machine, in which the material to be filled is conveyed by compressed air through a filling tube, has a storage cylinder which is closed at its underside by a grid-like floor having ventilation apertures. The filling tube is fitted above the floor in the peripheral wall of the storage cylinder. An improvement in the flow of the material to be filled and a more complete emptying on termination of the filling procedure are achieved if the floor is formed from at least three segments. Below the segments, sealed relative to one another, respective specifically associated compressed air supply chambers are disposed which are each provided with a regulatable compressed air supply.

Abstract: A bag-filling machine having an electronic weighing device which has a force receiver acting upon a bag support column. The machine also has a bag support guide which comprises two upper parallel guides and two lower parallel guides which are disposed in each instance on both sides of the bag support column and whose bearings are constructed as articulated heads. A possible lateral tilting of the bag support column is effectively prevented, without impairment of the vertical movement of this bag support column. The two upper parallel guides and the two lower parallel guides are rigidly connectd to one another by a respective coupling rod.

Abstract: Surprisingly active fragments of human pancreatic GRF have been synthesized which exhibit good biological activity. These synthetic peptides are extremely potent in stimulating the release of pituitary GH in humans and in nonhuman animals and have the general formula: H-Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser- Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Y wherein Y is NH.sub.2, Gln-NH.sub.2, Gln-Gln-NH.sub.2 or Gln-Gln-Gly-NH.sub.2. Two such fragments have been tested, namely the 29 and the 32 N-terminal residue sequences that are amidated at the C-terminus. These peptides, as well as nontoxic salts thereof, may be administered therapeutically to animals, including humans.

Abstract: Synthetic peptides are provided which are extremely potent in stimulating the release of pituitary GH in animals and which have the formula: H--R.sub.1 --Ala--Asp--Ala--Ile--Phe--Thr--R.sub.8 --Ser--R.sub.10 --Arg--R.sub.12 --R.sub.13 --Leu--R.sub.15 --Gln--Leu--R.sub.18 --Ala--Arg--Lys--Leu--Leu--R.sub.24 --R.sub.25 --Ile--R.sub.27 --R.sub.28 --Arg--Gln--Gln--Gly--Glu--R.sub.34 --Asn--Gln--Glu--R.sub.38 --R.sub.39 --R.sub.40 --Arg--R.sub.42 --R.sub.43 --Leu--Y wherein R.sub.1 is Tyr, Met, Leu, D--Tyr, D--His or His; R.sub.8 is Ser or Asn; R.sub.10 is Tyr or D--Tyr; R.sub.12 is Arg or Lys; R.sub.13 is Ile or Val; R.sub.15 is Gly or D--Ala; R.sub.18 is Tyr or Ser; R.sub.24 is His or Gln; R.sub.25 is Glu or Asp; R.sub.27 is Met, Ala, Nle, Ile, Leu or Val; R.sub.28 is Asn or Ser; R.sub.34 is Arg or Ser; R.sub.38 is Gln or Arg; R.sub.39 is Arg or Gly; R.sub.40 is Ser or Ala; R.sub.42 is Phe or Ala; R.sub.

Abstract: Rat hypothalamic GRF has been synthesized and has the formula: H-His-Ala-Asp-Ala-Ile-Phe-Thr-Ser-Ser-Tyr-Arg-Arg-Ile-Leu-Gly-Gln-Leu-Tyr- Ala-Arg-Lys-Leu-Leu-His-Glu-Ile-Met-Asn-Arg-Gln-Gln-Gly-Glu-Arg-Asn-Gln-Glu -Gln-Arg-Ser-Arg-Phe-Asn-OH. The peptide is believed to be and is hereinafter referred to as rhGRF (for rat hypothalamic GH releasing factor). The invention provides synthetic peptides which are extremely potent in stimulating the release of pituitary GH in animals and which have the formula: H-R.sub.1 -Ala-Asp-Ala-Ile-Phe-Thr-R.sub.8 -Ser-R.sub.10 -Arg-R.sub.12 -R.sub.13 -Leu-R.sub.15 -Gln-Leu-R.sub.18 -Ala-Arg-Lys-Leu-Leu-R.sub.24 -R.sub.25 -Ile-R.sub.27 -R.sub.28 -Arg-Gln-Gln-Gly-Glu-R.sub.34 -Asn-Gln-Glu-R.sub.38 -R.sub.39 -R.sub.40 -Arg-R.sub.42 -R.sub.43 -R.sub.44 -Y wherein R.sub.1 is Tyr, Met, D-Tyr, Leu, D-His or His; R.sub.8 is Ser or Asn; R.sub.10 is Tyr or D-Tyr; R.sub.12 is Arg or Lys; R.sub.13 is Ile or Val; R.sub.15 is Gly or D-Ala; R.sub.18 is Tyr or Ser; R.sub.24 is His or Gln; R.

Abstract: Human pancreatic GRF has been synthesized. The invention provides synthetic peptides which are extremely potent in stimulating the release of pituitary GH in mammals and which have the formula: H-Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-R.sub.15 -Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-S er-Asn-Gln-Glu-Arg-Gly-R.sub.40 -R.sub.41 -R.sub.42 -Y wherein R.sub.15 is Gly or D-Ala, R.sub.40 is Ala or des-R.sub.40, R.sub.41 is Phe or des-R.sub.41, R.sub.42 is des-R.sub.42 or 1 to 8 different amino acid residues selected from the group consisting of Gln, Gly, Ile, Leu, Lys, Pro, Thr and Val, and Y signifies the carboxyl moiety of the amino acid residue at the C-terminal and is the radical -COOR.sub.1,-CR.sub.1 O,-CONHNHR.sub.1,-CON(R.sub.1)(R.sub.2) or -CH.sub.2 OR.sub.1, with R.sub.1 and R.sub.2 being lower alkyl or hydrogen.

Abstract: rCRF (rat Corticotropin Releasing Factor) has been isolated, characterized and found to have the formula: H-Ser-Glu-Glu-Pro-Pro-Ile-Ser-Leu-Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Glu-Val- Leu-Glu-Met-Ala-Arg-Ala-Glu-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn-Arg-Lys-Leu -Met-Glu-Ile-Ile-NH.sub.2. Analogs are disclosed that are at least as potent as rCRF, and rCRF or these analogs orpharmaceutically or veterinarily acceptable salts thereof, dispersed in a pharmaceutically or veterinarily acceptable liquid or solid carrier, can be administered to animals, including humans, to achieve a substantial elevation of ACTH, .beta.-endorphin, .beta.-lipotropin, other products of the pro-opiomelanocortin gene and corticosterone levels and/or a lowering of blood pressure over an extended period of time. They may also be used as stimulants to elevate mood and improve memory and learning, as well as diagnostically.

Abstract: The peptide having the following formula has a potent effect on the reproduction processes of fish and is termed Fish GnRH:pGlu-His-Trp-Ser-Tyr-Gly-Trp-Leu-Pro-Gly-NH.sub.2.Spawning of teleostei fish can be promoted by administration of effective amounts of the peptide.

Abstract: CRF (Corticotropin Releasing Factor) has the formula:H-Ser-Gln-Glu-Pro-Pro-Ile-Ser-Leu-Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Glu-Val-L eu-Glu-Met-Thr-Lys-Ala-Asp-Gln-Leu-Ala-Gln-Gln-Ala-His-Ser-Asn-Arg-Lys-Leu- Leu-Asp-Ile-Ala-NH.sub.2.Analogs have been synthesized that are at least as potent as CRF, and CRF or these analogs or pharmaceutically acceptable salts thereof, dispersed in a pharmaceutically acceptable liquid or solid carrier, can be administered to mammals to achieve a substantial elevation of ACTH, .beta.-endorphin, .beta.-lipotropin and corticosterone levels and/or a lowering of blood pressure over an extended period of time. In the analogs, one or more of the first three N-terminal residues may be deleted or may be substituted by a peptide up to 10 amino acids long and/or by an acylating agent containing up to 7 carbon atoms. Ala in the 41-position may also be substituted or deleted so long as the remaining C-terminus is amidated. Several other substitutions may also be made throughout the chain.