Abstract: Disclosed are opioid peptides recovered from hydrolysates of wheat proteins with an acid protease and further a neutral or alkaline protease. Of those peptides, the structure of four opioid peptides was identified by the amino acid sequence of Gly-Tyr-Tyr-Pro (SEQ ID NO:1), Gly-Tyr-Tyr-Pro-Thr (SEQ ID NO:2), Gly-Tyr-Tyr-Pro-Thr-Ser (SEQ ID NO:3) or Tyr-Pro-Ile-Ser-Leu (SEQ ID NO:4). They are useful as a medicine such as narcotic, analgesic or the like.

Abstract: A feed for livestock, poultry and fishes for increasing a disease, pseudorabies resistance wherein a bile powder and bacterial cell containing peptidoglycan are mix in a basic feed in order to reduce losses due to infectious diseases including pseudorabies, by increasing the physical function of livestock, poultry and fishes using as little medicine as possible; and a feed additive for livestock, poultry and fishes including bile powder and bacterial cells containing peptidoglycan.

Abstract: Synthetic oligopeptides having potent anti-inflammatory and phospholipase A.sub.2 inhibiting properties are described. A method of controlling inflammation of body tissue is also described.

Abstract: A novel atrial peptide-degrading enzyme (ADE) is provided in isolated, purified form. The enzyme has a molecular weight of approximately 160,000 Daltons as measured by gel filtration chromatography, and is effective to cleave atrial peptides such as APII, APIII and ANF. Also provided are novel compounds useful as inhibitors of the enzyme and thus useful as blood pressure lowering agents, pharmaceutical compositions containing the inhibitors, and methods of using the inhibitors.

Abstract: The present invention deals with LHRH analogues which contain cytotoxic moieties and have influence on the release of gonadotropins from the pituitary gland of mammals, including humans. The compounds of this invention are represented by the formula:X--R.sup.1 --R.sup.2 --R.sup.3 -Ser-R.sup.5 --R.sup.6 (Q)-Leu-Arg-Pro-R.sup.10 --NH.sub.2whereinR.sup.1 is pGlu, Pro, D-Nal(2), or D-Phe(4Cl),R.sup.2 is His or D-Phe(4Cl),R.sup.3 is Trp, D-Trp or D-Pal(3),R.sup.5 is Tyr or Arg,R.sup.6 is D-Phe or R*.sup.6, where R*.sup.6 is D-Orn, D-Lys or D-Phe(NH.sub.2),R.sup.10 is Gly or D-Ala,X is hydrogen, a lower alkanoyl group of 2-5 carbon atoms or carbamyl,Q is bis-(2-chloroethyl)amino group provided that R.sup.6 is D-Phe,where R.sup.6 is R*.sup.6,Q is a complexed metal-containing acyl group having the formula: ##STR1## wherein Q' is Pt(Y).sub.

Abstract: Tripeptides, D-Phe-L-Pro-L-Arg-H, D-Phg-L-Pro-L-Arg-H and related compounds are purified in a process comprising 1) HPLC chromatography over an alkylsilane resin and elution with a gradient comprising an organic phase of between about 2% and about 40% of acetonitrile in an aqueous acidic phase containing an inorganic acid e.g. H.sub.2 SO.sub.4 and HCl, at a pH between about 2 and about 3, and 2) adjusting the pH of the acidic eluate with a water insoluble basic ion-exchange resin to about 4 to about 6.5. The purified peptides are useful antithrombotic agents.

Abstract: The present invention relates to a peptide having the amino acid sequence: Lys Arg Ser Thr Asn, Arg Arg Tyr Lys Glu Lys Glu Lys or Ala Ile Ile Pro Asp Arg Glu Val Leu Tyr and which peptide is capable of specifically binding to the antibody which is specific to the non-A, non-B hepatitis associated antigen. The peptide can be used as an anti-HCV antibody assay reagent with high sensitivity.

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

Abstract: Cell-free extracts from Pyrococcus furiosus were found to possess unusually high levels of proteolytic activity as measured by hydrolysis of azocasein; loss in activity was only 30% after incubation for 24 hours at 98.degree. C. and the half-life of proteolytic activity at that temperature was about 60 hours. Furthermore, cell-free extracts incubated at 98.degree. C. in 1% sodium dodecyl sulfate (SDS) for 24 hours yielded an SDS-resistant protease having a temperature optimum of at least 100.degree. C. The enzyme retained at least 40% of its activity when tested at 98.degree. C. by azocasein hydrolysis in the presence of 4M urea, 2M guanidinium chloride, 10 mM dithiothreitol or 150 mM .beta.-mercaptoethanol. The protease was found to have a pH optimum of 6.8 at 98.degree. C. and retained more than 45% of its activity at pH 9.3 and 82% of its activity at pH 4.5 in assays performed at those values.

Abstract: A biologically active peptide which includes the following structure:R.sub.1 --R.sub.1 --R.sub.1 --R.sub.3 --R.sub.5 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 R.sub.3 --R.sub.1 --R.sub.4 --R.sub.1 --R.sub.3 --R.sub.4 --R.sub.1 --R.sub.1.R.sub.1 is a hydrophobic amino acid, R.sub.2 is a basic hydrophilic amino acid, and R.sub.3 is a neutral hydrophilic amino acid, R.sub.4 is a hydrophobic or basic hydrophilic amino acid, and R.sub.5 is a hydrophobic, basic hydrophilic, or neutral hydrophilic amino acid.Examples of such peptides include the following:(SEQ ID NO:1)--NH.sub.2 ;(SEQ ID NO:2)--NH.sub.2 ;(SEQ ID NO:3)--NH.sub.2 ;(SEQ ID NO:4)--NH.sub.2 ;(SEQ ID NO:5)--NH.sub.2 ;(SEQ ID NO:6)--NH.sub.2 ;(SEQ ID NO:7)--NH.sub.2 ; and(SEQ ID NO:8).The peptides may be employed in pharmaceutical compositions.

Abstract: A high-absorbable transvaginal preparation having excellent absorbability of the active ingredient, which comprises a biologically active polypeptide and an absorption promoter comprising a polyoxyethylenealkylphenyl ether and one or more compounds selected from the group consisting of an N-acylamino acid, cholic acids, pectic acid, taurine, saccharin, glycyrrhizic acid, aspartame, or a salt thereof.

Abstract: A polypeptide comprising repeated amino acid sequences of a cell-adhesive protein represented by the formula:(Arg-Gly-Asp)n or (Tyr-Ile-Gly-Ser-Arg)nwherein n is a number ranging from 2 to 20; or a pharmaceutical acceptable salt thereof, which is valuable as an antimetastatic agent for cancer.

Abstract: The present invention provides methods and compositions for inducing penile erections, sufficient for vaginal penetration, in a human male suffering from impotence. When the impotence is substantially only neurogenic, psycogenic or neurogenic and psychogenic, a method of the invention comprises (A) administering to the male by intracavernosal injection peptide N-terminal histidine C-terminal methionineamide and (B) sexually stimulating the male. When the impotence is caused by severe atherosclerosis, a method of the invention comprises (A) administering to the male by intracavernosal injection an amount of a physiologically acceptable composition comprising (1) a neuropeptide selected from the group consisting of human vasoactive intestinal peptide and peptide N-terminal histidine C-terminal methionineamide and (2) an alpha-adrenergic blocker, such as phentolamine or prazosin, and (B) sexually stimulating the male.

Abstract: Vasoactive intestinal compound analogs containing substitutions of appropriately selected amino acids at specific positions of the VIP molecule.

Abstract: Analogs of CRF, which are based upon hCRF, oCRF and alpha-helical CRF, are disclosed that can be administered to achieve a substantial elevation of ACTH, .beta.-endorphin, .beta.-lipotropin, other products of the pro-opiomelanocortin gene and corticosterone levels. Analogs include those having the formula: Y-R.sub.1 -R.sub.2 -R.sub.3 -R.sub.4 -R.sub.5 -Ile-Ser-Leu-Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-R.sub.20 -R.sub.21 -R.sub.22 -R.sub.23 -R.sub.24 -R.sub.25 -Gln-Leu-Ala-Gln-Gln-Ala-R.sub.32 -Ser-Asn-Arg-Lys-Leu-R.sub.38 -R.sub.39 -Ile-R.sub.41 -NH.sub.2, wherein Y is an acyl group having 7 or fewer carbon atoms or hydrogen; R.sub.1 is Ser or desR.sub.1 ; R.sub.2 is Glu, Gln or desR.sub.2 ; R.sub.3 is Glu or desR.sub.3 ; R.sub.4 is Pro or desR.sub.4 ; R.sub.5 is Pro or desR.sub.5 ; R.sub.20 is Ala or Glu; R.sub.21 is Met or Nle; R.sub.22 is Ala or Thr; R.sub.23 is Arg or Lys; R.sub.24 is D-Ala or Ala; R.sub.25 is Glu or Asp; R.sub.32 is D-His or His; R.sub.38 is Met, Nle or Leu; R.sub.

Abstract: Derivatives of 1-phenyl pyrazolin-5-one have many applications for biomolecule synthesis. Enol esters of protected amino acids made by the present process provide efficient coupling in solid-phase peptide synthesis. The 1-phenyl-pyrazolin-5-one derivatives are highly crystalline, stable, non-toxic and easy to prepare. Many possess self-indicating properties, facilitating spectrophotometric monitoring and automation of peptide synthesis.

Abstract: This invention relates to peptide derivatives which are useful anticoagulant agents.

Abstract: The invention discloses a cyclic pentapeptide that inhibits metastasis of malignant cells.

Abstract: Peptide derivatives of the following general formula (I): Seq. ID Nos. 1-6. ##STR1## wherein AAA is deletion or Ser, BBB is deletion or Glu, CCC is deletion, Ile, Phe, Leu, cyclohexylalanine, D-alle or Lys substituted at the .epsilon.-position by C.sub.6 -C.sub.18 alkylcarbonyl group, DDD is Gly or Gln, EEE is Leu, Nle or Phe, FFF is Met, Leu or Nle, GGG is Ala, Ser, Leu, Asn, Asp or Gln, HHH is Leu, Glu or Lys, III is His, Lys or Arg, JJJ is His, Lys or Arg, Xaa is Ala modified at the carboxy terminal with an amino group, provided that CCC and DDD may independently be modified at the amino terminal by C.sub.2 -C.sub.