Abstract: The invention belongs to the technical field of polypeptide preparation methods, and in particular relates to a high-purity ACTH (human sequence) or analogue and large-scale preparation method thereof. The main steps include: amino acids are coupled from the C-terminal to the N-terminal by Fmoc solid-phase synthesis method to obtain the crude ACTH (human sequence) or analogue peptidyl-resin with protective groups, wherein the reaction temperature of C-15 peptide synthesis is 40-60° C. After cleavge and precipitation, the crude product of ACTH (human sequence) or analogue is obtained, and then the high-purity product is obtained by liquid chromatography. The chromatographic purity of ACTH (human sequence) or analogue prepared by the invention is more than 99%, the stability is good, and the yield of the target peptide is ?63%.

Abstract: Provided herein are methods for prophylactic treatment of renal disorders comprising administration of adrenocorticotropic hormone (ACTH), or fragment, analog, complex or aggregate thereof, or any combination thereof, to an individual suspected of having, predisposed to, or at risk of developing a renal disorder.

Abstract: Novel polypeptides and methods of making and using the same are described herein. The polypeptides include cross-linking (“hydrocarbon stapling”) moieties to provide a tether between two amino acid moieties, which constrains the secondary structure of the polypeptide. The polypeptides described herein can be used to treat diseases characterized by excessive or inadequate cellular death.

Abstract: The present invention relates to a molecule capable of binding to adrenocorticotropic hormone (ACTH) with high affinity. The present invention also relates to use of the molecule for detection and/or purification of ACTH.

Abstract: Provided herein are methods for prophylactic treatment of renal disorders comprising administration of adrenocorticotropic hormone (ACTH), or fragment, analog, complex or aggregate thereof, or any combination thereof, to an individual suspected of having, predisposed to, or at risk of developing a renal disorder.

Abstract: Novel polypeptide derivatives having protracted profile of action.

Abstract: The present invention relates to therapeutic regimens or protocols designed for the treatment, management or prevention of edema. In particular, the invention pertains to methods of treating or managing edema associated with brain tumors involving the administration of a therapeutically effective amount of corticorelin acetate that achieves a steroid-sparing effect.

Abstract: Provided is a factor capable of inducing enucleation, which is a final stage of erythrocyte differentiation, within a short time. More particularly, provided are a method of inducing enucleation, which is a final stage of erythrocyte differentiation, within a short time by adding a compound derived from proopiomelanocortin (POMC) to an undifferentiated (nucleated) erythrocyte, and an enucleation inducer including the compound.

Abstract: The invention is directed to a pharmacologically active peptide conjugate having a reduced tendency towards enzymatic cleavage comprising a pharmacologically active peptide sequence (X) and a stabilising peptide sequence (Z) of 4-20 amino acid residues covalently bound to X.

Abstract: A human urocortin-related peptide with significant sequence homology to the CRF neuropeptide family was identified. A mouse cDNA was isolated from whole brain poly (A+) RNA that encodes a predicted 38 amino acid peptide protein designated herein as urocortin II. Both human URP and mouse Ucn II are structurally related to the other known mammalian family members, CRF and urocortin (Ucn). These peptides are involved in the regulation of the hypothalamic-pituitary-adrenal axis under basal and stress conditions, suggesting a similar role for URP and Ucn IL Synthesized Ucn-II and URP peptide binds with higher affinity to CRF-R2 than to CRF-R1 Ucn II and human URP appear to be involved in the regulation of body temperature and appetite and may play a role in other stress related phenomenon. These findings identify Ucn II and human URP as a new members of the CRF family of neuropeptides, which are expressed centrally and bind to CRF-R2.

Abstract: ACTH analog compounds of the present invention include compounds comprising an ACTH peptide sequence with one or more structural modifications that can have one or more of the following preferred ACTH analog biological functions: (1) reduction of corticosteroid secretion by adrenal membrane in the presence of the ACTH analog compared to unmodified ACTH, (2) reduction of corticosteroid secretion by adrenal membrane in the presence of endogenous ACTH and (3) increased MC-2R binding affinity with reduced activation of the MC-2R receptor compared to unmodified ACTH binding to the MC-2R melanocortin. The ACTH analog compounds of the present invention are therefore useful for treatment or prevention of diseases and disorders related to ACTH, ACTH receptors or corticosteroid secretion, such as premature labor and Cushing's Disease.

Abstract: The present invention relates to conjugates of CRF that have been modified to include a moiety that protects CRF from degradation and prolongs the half-life of CRF.

Abstract: The present invention relates to compositions containing unacylated ghrelin and derivatives thereof and their uses in the control of glycemia in ageing patients, GH deficient patients, diabetic patients and obese patients.

Abstract: Novel cyclic and linear peptides of the formula R1—X—X1—X2—X3—X4—X5—X6—X7—X8—X9—X10—X11—R2 are useful in the treatment of obesity are provided.

Abstract: The present invention relates to compounds comprising modified corticotrophin releasing factor peptide and specifically urocortin and urocortin-related peptides, modified derivatives thereof, and conjugates of such modified peptides and derivatives to serum components, preferably serum proteins or peptides. The compounds and conjugates of the invention comprise a reactive group, which is covalently attached to a modified peptide or derivative, optionally through a linking group. The present invention also provides methods for the covalent attachment of a modified peptide or derivative to a serum protein or peptide to form a conjugate of the invention. The conjugates of the invention preferably exhibit a longer in vivo circulating half-life compared to the corresponding unconjugated peptides. The conjugates of the invention also retain at least some of the biological activity of the unconjugated peptides, and preferably exhibit increased biological activity compared to the unconjugated peptides.

Abstract: The present invention identifies four new isoforms of human corticotropin releasing hormone receptor type 1 (CRH-R1e, 1f, 1g and 1h) and three new isoforms of mouse corticotropin releasing hormone receptor type 1 (mCRH-R1c, 1e and 1f). The data indicate that polymorphism of CRH-R1 expression is related to anatomic location, skin physiological or pathologic status, specific cell type, external stress (UV), and that cAMP dependent pathways and TPA may regulate CRH-R1.

Abstract: The present invention provides pro-micelle compositions comprising a pharmaceutically active agent encapsulated with a membrane of esterified C12-C18 fatty acids. In the mammalian intestine, exposure to C12-C18 fatty acids results in conversion of the pro-micelle to a stable micelle that effectively delivers the pharmaceutically active agent to the systemic circulation. The present invention further provides methods of making and using such compositions.

Abstract: Genetically-encodable, environmentally-responsive fusion proteins comprising ELP peptides. Such fusion proteins exhibit unique physico-chemical and functional properties that can be modulated as a function of solution environment. The invention also provides methods for purifying the FPs, which take advantage of these unique properties, including high-throughput purification methods that produce high yields (e.g., milligram levels) of purified proteins, thereby yielding sufficient purified product for multiple assays and analyses. The high throughput purification technique is simpler and less expensive than current commercial high throughput purification methods, since it requires only one transfer of purification intermediates to a new multiwell plate.

Abstract: The glutamic acid residue of corticotropin-releasing hormone analogs have had the position 20 amino acid residue replaced with a D-amino acid moiety. The resulting CRH analogs do not significantly lower blood pressure but have anti-proliferative actions in cell culture and inhibit experimental cancer growth in animals (mice and rats). Novel applications of such analogs are described, such as to inhibit abnormal cell proliferation for conditions such as cancer, including melanoma, and for inflammatory dermatoses, such as psoriasis.

Abstract: Mammalian kringle 5 fragments and kringle 5 fusion proteins are disclosed as a compounds for treating angiogenic diseases. Methods and compositions for inhibiting angiogenic diseases are also disclosed.

Abstract: Methods for treating sexual dysfunction, such as erectile dysfunction or sexual arousal disorder, with a compound having the generic formula X1—X2-(D)Phe-Arg-(D)Trp-X3. A particularly useful compound is HP-228, which has the formula Ac-Nle-Gln-His-(D)Phe-Arg-(D)Trp-Gly-NH2. The invention also provides methods for selecting melanocortin receptor-3 ligands by determining whether a compound modulates the activity of MC-3 as an agonist or antagonist. These methods can be used to screen compound libraries for ligands to treat MC-3-associated conditions. Such conditions include sexual dysfunction, including erectile dysfunction and sexual arousal disorder.

Abstract: Bivalent agonists having affinity for one or more G-protein coupled receptors, comprising two agonist or two antagonist ligand domains, wherein the distance between the ligand domains can range from about 40 to about 250 Å, and further comprising a backbone, wherein the backbone is covalently bonded to the two ligand domains, are provided. Additionally, bivalent agonists are provided that comprise one agonist and one antagonist ligand domain. In a specific embodiment, the bivalent agonists are peptide dimers, wherein the backbone comprises two spacer regions, two polylysine regions, and a disulfide bond region, such that the order in which the ligand domains, spacer regions, polylysine regions and disulfide bond region are covalently bonded together is: (ligand domain)-(spacer region)-(polylysine region)-(disulfide bond region)-(polylysine region)-(spacer region)-(ligand domain). Such peptide dimers are prepared from oxidative dimerization of their corresponding monomers.

Abstract: Novel DNA fragments encoding novel polypeptides having properties of melanotropic hormone receptors, especially DNA molecules encoding melanocyte stimulating hormone receptors (MSH receptors), as well as polypeptides which are MSH receptors, are disclosed. The use and engineering of melanotropic hormone receptor DNA and polypeptides for production of monoclonal antibodies for diagnostic and therapeutic purposes, as well as the engineering of drugs, cell lines, vectors, and DNA for therapeutic and diagnostic purposes are also disclosed.

Abstract: Novel cyclic CRF agonist peptides have the amino acid sequence: (cyclo 30-33)Ac-Ser-Leu-Asp-Leu-Thr-D-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-Glu-Nle-Ala-Arg-Ala-Glu-Gln-Leu-Ala-Gln-Glu-Ala-R32-R33-Asn-Arg-Lys-Leu-Nle-Glu-Ile-Ile-NH2 wherein R32 is His, D-His or an equivalent &agr;-amino acid; R33 is Lys or Orn. The N-terminus may be extended by Tyr, D-Tyr or Ile. Lys may be substituted for Arg23, and its side chain connected by a lactam bridge to Glu20 to form a bicyclic peptide. Certain disclosed CRF agonists include: (cyclo 30-33)[Ac-Ser7, D-Phe12, Nle21,38, Glu30, Lys33]r/hCRF(7-41); (cyclo 30-33)[Ac-Ser7, D-Phe12, Nle21,38, Glu30, D-His32, Lys33]r/hCRF(7-41); (bicyclo 20-23, 30-33)[Ac-Ser7, D-Phe12, Nle21,38, Lys23,33, Glu30, D-His32]-r/hCRF(7-41); (cyclo 30-33)[Ac-Ser7, D-Phe12, Nle18,21, Glu30, D-Ala32, Lys33]&agr;-helicale CRF(7-41); and (cyclo 30-33)[Ac-Ser7, D-Phe12, Nle21,38, CML27,40, Glu30, Lys33]r/hCRF(7-41).

Abstract: Novel cyclic CRF antagonist peptides are created by shortening the N-terminus of a CRF family peptide by 8 residues and adding an acyl group. CML is present in what would be the 27-position of the native CRF sequence, and a cyclizing bond is created between the side chains of the residues in positions 30 and 33. The side chain of Lys, preferably, in position 33 is linked to the side chain of Glu in position 30 by a lactam bridce. Disclosed CRF antagonists include: (cyclo 30-33)[Ac-Asp9, D-Phe12, Nle21,38, CML27,40, Glu30, Lys33]r/hCRF(9-4); (cyclo 30-33)[Ac-Asp9, D-Phe12, CML18,27, Nle21,38, Glu30, Lys33]r-hCRF(9-41); (cyclo 30-33)[Ac-Asp9, D-Phe12, Nle21,38, CML27,37, Glu30, Lys33]r/hCRF(9-41); (cyclo 30-33)[Ac-Asp9, D-Phe12, CML14,27, Nle21,38, Glu30, Lys33]r/hCRF(9-41); (cyclo 30-33)[Ac-Asp9, D-Phe12, Nle21,38, CML27, Glu30, Lys33]r/hCRF(9-41); and (cyclo 30-33)[Ac-Asp9, D-Phe12, Nle21,38, CML27,40, Glu30, Aib32, Lys33]r/hCRF(9-41).

Abstract: The glutamic acid residue of corticotropin-releasing hormone analogs have had the position 20 amino acid residue replaced with a D-amino acid moiety. The resulting CRH analogs do not significantly lower blood pressure but have anti-proliferative actions in cell culture and inhibit experimental cancer growth in animals (mice and rats). Novel applications of such analogs are described, such as to inhibit abnormal cell proliferation for conditions such as cancer, including melanoma, and for inflammatory dermatoses, such as psoriasis.

Abstract: Genes encoding melanocortin receptors have been identified, isolated, cloned and localized to their chromosomal positions. These genes have been used to transfect mammalian cells lacking endogenous melanocortin receptors to induce expression. Additionally, melanocortin receptor binding, secondary signalling, and tissue distribution has been characterized. The genes and their gene products may therefore be used to to provide therapeutic vehicles for the treatment of processes involving the function of melanocortin receptors.

Abstract: The present invention provides recombinant expression constructs comprising nucleic acid encoding mammalian melanocortin receptors, and mammalian cells into which said recombinant expression constructs have been introduced that express functional mammalian melanocortin receptors. The invention provides a panel of such transformed mammalian cells expressing melanocortin receptors for screening compounds for receptor agonist and antagonist activity. The invention also provides methods for using such panels of melanocortin receptor-expressing mammalian cells to specifically detect and identify agonists and antagonists for each melanocortin receptor, as well as patterns of agonist and antagonist activity of said compounds for the class of melanocortin receptors. Such screening methods provide a means for identifying compounds with patterns of melanocortin agonist and antagonist activity which are associated with the capacity to influence or modify metabolism and behavior, particularly feeding behavior.

Abstract: A combination of insulin and an insulin-like growth factor I (IGF-I) as used in the manufacture of a medicament for counteracting a decrease in nitrogen balance and for counteracting a decrease in protein synthesis. The medicament can be used for the treatment of catabolism which is a protein catabolism due to glucocorticoid excess.

Abstract: Novel cyclic CRF antagonist peptides have the amino acid sequence: ##STR1## wherein Y is Ac, H, Ac-Thr or H-Thr; R.sub.30 is Glu or Cys; R.sub.32 is His or preferably a basic and/or aromatic D-amino acid such as D-His or D-Arg; R.sub.33 is Lys, Orn or Cys. The N-terminus may be extended by Leu or Asp-Leu. CML may be substituted for Leu.sup.27, and D-Tyr may be substituted for D-Phe to facilitate labelling. Lys may be substituted for Arg.sup.23, and its side chain connected by a lactam bridge to Glu.sup.20 to form a bicyclic peptide. Disclosed CRF antagonists include:(cyclo 30-33)?D-Phe.sup.12, Nle.sup.21,38, Glu.sup.30, Lys.sup.33 !r/hCRF(12-41),(cyclo 30-33)?Ac-Thr.sup.11, D-Phe.sup.12, Nle.sup.21,38, Glu.sup.30, Lys.sup.33 !r/hCRF(11-41),(cyclo 30-33)?D-Phe.sup.12, Nle.sup.21,38, Cys.sup.30,33 !r/hCRF(12-41),(bicyclo 20-23,30-33)?D-Phe.sup.12, Nle.sup.21,38, Lys.sup.23,33, Glu.sup.30 !-r/hCRF(12-41),(cyclo 30-33)?D-Phe.sup.12, Nle.sup.21,38, Glu.sup.30, D-His.sup.32, Lys.sup.

Abstract: Peptide analogues are provided with amino acid sequences of the corticotropin-releasing factor superfamily, but having at least one amino acid residue that has been replaced with a D-amino acid residue or a D-amino acid analog. The peptide analogues have anti-inflammatory activity while having a receptor selectivity and thus a disassociated ACTH response.

Abstract: The present invention relates to a mammalian alpha-melanocyte stimulating hormone receptor. The invention is directed toward the isolation, characterization and pharmacological use of mammalian melanocyte stimulating hormone receptor, the gene corresponding to this receptor, a recombinant eukaryotic expression construct capable of expressing a mammalian melanocyte stimulating hormone receptor in cultures of transformed eukaryotic cells and such cultures of transformed eukaryotic cells that synthesize mammalian melanocyte stimulating hormone receptor. The invention also provides methods for screening MSH-R agonists and antagonists in vitro using preparations of receptor from such cultures of eukaryotic cells transformed with a recombinant eukaryotic expression construct comprising the MSH-R receptor gene. The invention specifically provides human and mouse MSH-R genes.

Abstract: Novel cyclic CRF agonist peptides have the amino acid sequence: (cyclo 30-33)Ac-Pro-Pro-Ile-Ser-Leu-Asp-Leu-Thr-D-Phe-His-Leu-Leu-Arg-Glu-Val-Leu -Glu-Nle-Ala-Arg-Ala-Glu-Gln-Leu-Ala-Gln-R.sub.30 -Ala-R.sub.32 -R.sub.33 -Asn-Arg-Lys-Leu-Nle-Glu-Ile-Ile-NH.sub.2 wherein R.sub.30 is Glu or Cys; R.sub.32 is His or a D-amino acid such as D-His, D-Arg or similar; R.sub.33 is Lys, Orn or Cys. The N-terminus may be extended by Ser-Glu-Glu. Lys may be substituted for Arg.sup.23, and its side chain connected by a lactam bridge to Glu.sup.20 to form a bicyclic peptide. Certain disclosed CRF agonists include:(cyclo 30-33)?Ac-Pro.sup.4, D-Phe.sup.12, Nle.sup.21,38, D-His.sup.32, Glu.sup.30, Lys.sup.33 !r/hCRF(4-41),(cyclo 30-33)?Ac-Pro.sup.4, D-Phe.sup.12, Nle.sup.21,38, D-His.sup.32, Glu.sup.30, Orn.sup.33 !r/hCRF(4-41),(cyclo 30-33)?Ac-Pro.sup.4, D-Phe.sup.12, Nle.sup.21,38, Cys.sup.30,33, D-His.sup.32 !r/hCRF(4-41),(bicyclo 20-23,30-33)?Ac-Pro.sup.4, D-Phe.sup.12, Nle.sup.21,38, Lys.sup.23,33, Glu.sup.30, D-His.sup.

Abstract: The invention features a substantially pure preparation of a peptide having corticotropin release inhibiting factor (CRIF) activity comprising at least three contiguous amino acids contained within the amino acid sequence positioned between the fourth and fifth thyrotropin releasing hormone (TRH) sequence on a prepro-TRH protein. The CRIF peptide further comprises the fourth uncleaved TRH portion of prepro-TRH positioned at the amino terminus of CRIF. Compositions, methods of diagnosis and methods of treating CRIF related diseases are also included in the invention.

Abstract: Novel cyclic CRF agonist peptides have the amino acid sequence: (cyclo 30-33)Ac-Pro-Pro-Ile-Ser-Leu-Asp-Leu-Thr-D-Phe-His-Leu-Leu-Arg-Glu-Val-Leu -Glu-Nle-Ala-Arg-Ala-Glu-Gln-Leu-Ala-Gln-R.sub.30 -Ala-R.sub.32 -R.sub.33 -Asn-Arg-Lys-Leu-Nle-Glu-Ile-Ile-NH.sub.2 wherein R.sub.30 is Glu or Cys; R.sub.32 is His, D-His or an equivalent .alpha.-amino acid; R.sub.33 is Lys, Orn or Cys. The N-terminus may be extended by Ser-Glu-Glu or shortened by up to three more residues. Lys may be substituted for Arg.sup.23, and its side chain connected by a lactam bridge to Glu.sup.20 to form a bicyclic peptide. Certain disclosed CRF agonists include:(cyclo 30-33)?Ac-Pro.sup.4, D-Phe.sup.12, Nle.sup.21,38, Glu.sup.30, D-His.sup.32, Lys.sup.33 !r/hCRF(4-41),(cyclo 30-33)?Ac-Ser.sup.7, D-Phe.sup.12, Nle.sup.21,38, Glu.sup.30, Lys.sup.33 !r/hCRF(7-41),(cyclo 30-33)?Ac-Ser.sup.7, D-Phe.sup.12, Nle.sup.21,38, Glu.sup.30, D-His.sup.32, Lys.sup.33 !r/hCRF(7-41),(bicyclo 20-23, 30-33)?Ac-Pro.sup.4, D-Phe.sup.12, Nle.sup.21,38, Lys.sup.

Abstract: Novel cyclic CRF antagonist peptides are created by shortening the N-terminus of a CRF family peptide by 8-11 residues and adding an acyl group. CML is preferably present in what would be the 27-position of the native CRF sequence, and D-Tyr may be incorporated at the N-terminus to facilitate labelling. The cyclizing bond is preferably created between the side chains of the residues in positions 30 and 33; but it may alternatively be created between the residues in either of positions 28 and 29 with those in positions 31 and 32 or with those in positions 32 and 33, respectively. The side chain of Lys in position 33 is preferably linked to the side chain of Glu in position 30 by a lactam bridge to form the cyclic peptide. Disclosed CRF antagonists include:(cyclo 30-33) ?Ac-Asp.sup.9, D-Phe.sup.12, Nle.sup.21,38, CML.sup.27,40, Glu.sup.30, Lys.sup.33 !r/hCRF(9-41),(cyclo 30-33) ?Ac-Asp.sup.9, D-Phe.sup.12, Nle.sup.21,38, CML.sup.27,37, Glu.sup.30, Lys.sup.33 !r/hCRF(9-41),(cyclo 30-33) ?Ac-Asp.sup.9, D-Phe.sup.

Abstract: A human growth hormone can be purified by allowing a solution containing the human growth hormone to contact with a blue pigment-bonded carrier in order to selectively adsorb the human growth hormone, then eluting the human growth hormone with an eluant of high ionic strength or an eluant containing a protein denaturing agent. This method readily enables the mass production of a highly purified human growth hormone.

Abstract: A method is disclosed for counteracting a decrease in nitrogen balance and counteracting a decrease in protein synthesis in an individual, comprising administering to the individual a combination of insulin and IGF-I.

Abstract: Improved CRF antagonist peptides have the formula: ##STR1## wherein R.sub.30 is Cys or Glu; R.sub.33 is Cys, Lys or Orn; provided that when R.sub.30 is Cys, R.sub.33 is Cys and when R.sub.30 is Glu, R.sub.33 is Lys or Orn. The N-terminus may be extended by Asp-Leu-Thr. Lys may be substituted for Arg.sup.23 and its side chain connected by a lactam bridge to Glu.sup.20 to form a dicyclic peptide. Specific CRF antagonists disclosed include (cyclo 30-33) [D-Phe.sup.12, Nle.sup.21,38, Glu.sup.30, Lys.sup.33 ]rCRF(12-41); (cyclo 30-33) [D-Phe.sup.12, Nle.sup.21,38, Glu.sup.30, Orn.sup.33 ]rCRF(12-41), (cyclo 30-33) [D-Phe.sup.12, Nle.sup.21,38, Cys.sup.30,33 ]rCRF (12-41) and (bicyclo 20-23,30-33) [D-Phe.sup.12, Nle.sup.21,38, Lys.sup.23,33, Glu.sup.30 ]-rCRF(12-41).

Abstract: Isolated, substantially pure mammalian brain-derived membrane-associated CRF-binding proteins and biologically active fragments thereof are provided as well as isolated and purified DNA fragments which encode the CRF binding proteins or biologically active fragments thereof or homologs of other mammalian species. By administering an amount of such CRF binding protein or a fragment thereof effective to modulate receptor activation, it is possible to modulate the action of CRF upon (a) the brain and nervous system, (b) the pituitary particularly for production of ACTH, beta endorphin and cortisol, (c) sites of inflammation, (d) the placenta, (e) the adrenal glands, (f) the gonads or (g) the gastrointestinal tract. Administration of an N-terminal fragment of the protein increases the binding site density for CRF and thus modulates its biological effect in vivo.

Abstract: Peptide derivatives containing one or more substituents separately linked by an amide, amino or sulfonamide bond to an amino group on either the N-terminal end or side chain of a biologically active peptide moiety. The peptide derivatives have relatively enhanced biological activity when compared to the corresponding peptide alone.

Abstract: Disclosed are improved CRF peptide antagonists such as those having the formula: Y-D-Phe-Xaa.sub.13 -Leu-Leu-Arg-Xaa.sub.17 -Xaa.sub.18 -Leu-Xaa.sub.20 -Nle-Xaa.sub.22 -Xaa.sub.23 -Xaa.sub.24 -Xaa.sub.25 -Xaa.sub.26 -Leu-Xaa.sub.28 -Xaa.sub.29 -Gln-Xaa.sub.31 -Xaa.sub.32 -Xaa.sub.33 -Xaa.sub.34 -Arg-Xaa.sub.36 -Xaa.sub.37 -Nle-Xaa.sub.39 -Xaa.sub.40 -Xaa.sub.41 -NH.sub.2 wherein Y is Ac or hydrogen; Xaa.sub.13 is His, Tyr or Glu; Xaa.sub.17 is CML, Glu, Asn or Lys; Xaa.sub.18 is Val, Nle or Met; Xaa.sub.20 is Glu, D-Glu, Aib or D-Ala; Xaa.sub.22 is Ala, Aib, Thr, Asp or Glu; Xaa.sub.23 is Arg, Orn, Har or Lys; Xaa.sub.24 is Ala or Aib; Xaa.sub.25 is Asp or Glu; Xaa.sub.26 is Gln, Asn or Lys; Xaa.sub.28 is Ala or Aib; Xaa.sub.29 is Gln, Aib or Glu, Xaa.sub.31 is Ala or Aib; Xaa.sub.32 is His, Aib, Gly, Tyr or Ala; Xaa.sub.33 is Ser, Aib, Asn, Leu, Thr or Ala; Xaa.sub.34 is Asn or Aib; Xaa.sub.36 is Lys, Orn, Arg, Har or Leu; Xaa.sub.37 is Leu or Tyr; Xaa.sub.39 is Glu, Aib or Asp; Xaa.sub.

Abstract: Improved CRF peptide antagonists have the formula: ##STR1## wherein R.sub.20 is Cys or Glu; R.sub.23 is Cys, Lys or Orn; provided that when R.sub.20 is Cys, R.sub.23 is Cys and when R.sub.20 is Glu, R.sub.23 is Lys or Orn; or a nontoxic addition salt thereof. Specific CRF antagonists disclosed include (cyclo 20-23) [D-Phe.sup.12, Lys.sup.23, Nle.sup.21,38, ]rCRF(12-41); (cyclo 20-23) [D-Phe.sup.12, Orn.sup.23, Nle.sup.21,38 ]rCRF(12-41) and (cyclo 20-23) [D-Phe.sup.12, Cys.sup.20, Cys.sup.23, Nle.sup.21,38 ]rCRF(12-41).

Abstract: Administration of a corticotropin-releasing factor (or a salt or analog thereof) decreases the leakage of blood components into tissues produced by various adverse medical conditions. Thus, treatments with corticotropin-releasing factor are useful in systemic inflammatory conditions.

Abstract: The present invention relates to a process for manufacturing a composition highly containing .alpha.-lactalbmin. This process comprises adjusting, to pH of 2-4 or 5 or higher, cheese whey, acid casein whey or rennet casein whey; contacting the whey with an ion exchanger, to produce an exchanger-passed solution; and then, concentrating and/or desalting the exchanger-passed solution, if necessary after the exchanger-passed solution is adjusted to a pH of 4 or lower. According to the present process, it is possible to efficiently produce a high .alpha.-lactalumin content composition at low cost and in a simple and easy manner on an industrial scale. The resultant high .alpha.-lactalumin content composition can be used for food materials and medical materials.

Abstract: An orally administered complex of a drug, hormone, bio-active peptide, or immunogen with the carrier molecule, such as vitamin B12 or analogue thereof, and a method for delivering said complex to the intestine of a host vertebrate in order to deliver the complex to the circulation of the host and thereby elicit a pharmacological response to the drug, hormone, or bio-active molecule or to elicit a systemic immune response to the immunogen. The invention also provides a method for the production of the complex. Further the invention provides medicaments containing the complex.

Abstract: Processes for synthesizing polypeptides containing substantially non-antigenic polymers, preferably poly(alkylene glycols) in specifically predetermined sites are disclosed. Polypeptides prepared by such processes acre also disclosed.

Abstract: Pharmaceutical compositions containing ACTH(1-24) are effective in the treatment of shock conditions and of respiratory and cardiocirculatory insufficiency. The compositions of the invention may be administered by parenteral or inhalatory route at a dosage ranging from 1 to 10 mg of active principle.

Abstract: Administration of a Corticotropin-Releasing Factor (or a salt or analog thereof) decreases the leakage of blood components into brain tissue produced by various adverse medical conditions and reduces bleeding when muscle tissues are cut and handled, such as in plastic and reconstructive surgery. A method of treating a patient for injury to or disease of the brain, central nervous system, or musculature in which edema is a factor comprises administering to the patient a Corticotropin-Releasing Factor (or a salt or analog) in an amount effective to decrease vascular permeability in the injured or diseased brain, nervous system tissue or musculature, and thereby to reduce edema. Administration in accordance with the method can be about two hours before surgery, or can be up to three days after injury.

Abstract: A composition is disclosed which comprises a solution of human serum albumin essentially free of chemicals used in processing. The preparation is also essentially free of metals such as aluminum. The composition is 100% pure by cellulose acetate electrophoresis and is essentially monomeric when tested by high pressure liquid chromatography. The turbidity is less than 5 N.T.U. (National Turbidity Units). This preparation has a substantially longer shelf life and remains biologically active longer than products currently available. The novelty of this product is also such that it does not leach metallic substances such as aluminum from its closure. Novel applications of process methodology are taught in the preparation of this composition and a novel preparation results from essentially non hemoglobin containing albumin sources such as Source Plasma (Human).