Abstract: According to the present invention, adrenomedullin which is a novel peptide having a hypotensive effect; proadrenomedullin N-terminal 20 peptide (proAM-N20) corresponding to an amino acid sequence of an N-terminus of proadrenomedullin, having a catecholamine secretion inhibitory effect; proadrenomedullin N-terminal 10-20 peptide (proAM-N(10-20)) having a Na channel inhibitory effect, and a gene encoding these peptides are provided. In addition, according to the present invention, these peptides in a sample containing adrenomdullin or proAM-N20 in an unknown amount can be quantified by using an antibody against adrenomedullin, proAM-N20, or its fragment.

Abstract: According to the present invention, adrenomedullin which is a novel peptide having a hypotensive effect; proadrenomedullin N-terminal 20 peptide (proAM-N20) corresponding to an amino acid sequence of an N-terminus of proadrenomedullin, having a catecholamine secretion inhibitory effect; proadrenomedullin N-terminal 10-20 peptide (proAM-N(10-20)) having a Na channel inhibitory effect, and a gene encoding these peptides are provided. In addition, according to the present invention, these peptides in a sample containing adrenomdullin or proAM-N20 in an unknown amount can be quantified by using an antibody against adrenomedullin, proAM-N20, or its fragment.

Abstract: A C-terminal .alpha.-amidating enzyme of Xenopus laevis and precursor thereof produced by a recombinant DNA technique; a DNA coding for the enzyme or precursor thereof; a plasmid containing the DNA; a host organism transformed with the plasmid; a process for production of the enzyme using the transformant; and a process for production of a C-terminal .alpha.-amidated peptide using the enzyme.

Abstract: According to the present invention, adrenomedullin which is a novel peptide having a hypotensive effect; proadrenomedullin N-terminal 20 peptide (proAM-N20) corresponding to an amino acid sequence of an N-terminus of proadrenomedullin, having a catecholamine secretion inhibitory effect; proadrenomedullin N-terminal 10-20 peptide (proAM-N(10-20)) having a Na channel inhibitory effect, and a gene encoding these peptides are provided. In addition, according to the present invention, these peptides in a sample containing adrenomedullin or proAM-N20 in an unknown amount can be quantified by using an antibody against adrenomedullin, proAM-N20, or its fragment.

Abstract: Novel peptides represented by the general formula: ##STR1## and physiologically acceptable acid addition salts thereof; where (A) represents H-, H-Gly, H-Lys-Gly, H-Ser-Lys-Gly, H-Leu-Ser-Lys-Gly, H-Gly-Leu-Ser-Lys-Gly, H-ser, H-Ser-Ser, H-Arg-Ser-Ser, H-Arg-Arg-Ser-Ser, H-Leu-Arg-Arg-Ser-Ser, H-Ser-Leu-Arg-Arg-Ser-Ser;(B) represents H-Cys or Pmp;(C) represents Phe-, pCl-Phe, pF-Phe, pNO.sub.2 -Phe or Cha;(D) represents Ile, Val, Aib, tLeu, Gly or Leu;(E) represents Lys or Arg;(F) represents Ile, Leu or Met;(G) represents Ser or Ala;(H) represents Met or Gln;(I) represents --OH, -Asn-OH, -Asn-Ser-OH, -Asn-Ser-Phe-OH, -Asn-Ser-Phe-Arg-OH or -Asn-Ser-Phe-Arg-Tyr-OH; and the symbol " . . . " represents a disulfide bond;provided that 1) .alpha.-hANP, 2) .alpha.-hANP (7-28) and 3) CNP-22 are excluded from the scope of that general formula.Also disclosed are agents for suppressing the growth of vascular smooth muscle cells that contains those peptides as effective ingredients.

Abstract: The invention relates to a C-terminal .alpha.-amidating enzyme of porcine origin having the following properties: (1) the action is on a peptide or protein represented by the formula:X-R-Gly,wherein Gly represents a C-terminal glycine residue, R represents an amino acid residue to be .alpha.-amidated, and X represents a remaining portion of the peptide or protein to convert it to a peptide or protein represented by the formula:X-R-NH.sub.2,wherein R-NH.sub.2 represents a C-terminal .alpha.-amidated amino acid residue and X represents a remaining portion of the peptide or protein; (2) the optimal pH is 6.5 to 8.5; (3) the molecular weight is about 92,000 as determined by SDS-polyacrylamide gel electrophoresis; and (4) it contains the following peptide fragment:. . . Glu-Ala-Pro-Leu-Leu-Ile-Leu-Gly . . . .Further, the invention relates to a process for the production of the C-terminal .alpha.

Abstract: There are disclosed a new peptide .alpha.-hANP of the following structure: ##STR1## and acid addition salt thereof; a diuretic composition and a hypotensor composition containing the .alpha.-hANP or an acid addition salt thereof; and processes for the production thereof.

Abstract: Disclosed are a novel physiologically active peptide having the following structural formula and an acid addition salt thereof: ##STR1## (where (1)/(2) and (3)/(4) are respectively bonded directly and each of the cysteine residues (Cys) at positions 6 and 22 forms an intramolecular S--S bond).This novel peptide derives from porcine and since it exhibits natriuretic and hypotensive actions, the peptide is useful as a therapeutic for cardiac edema, nephredema, hepatic edema, hypertension, congestive heart failure, acute and chronic renal insufficiency, etc. Further, exhibiting the capability of suppressing the growth of smooth vascular muscle cells and the cGMP producing activity, the novel peptide is anticipated to have the potential for serving as an effective therapeutic for atherosclerosis.

Abstract: A peptide composed of 53 amino acid residues represented by the following amino acid sequence: (see SEQ ID NO: 1) ##STR1## and derivatives thereof represented by the following amino acid sequence: (see SEQ ID NO: 2) ##STR2## wherein X is as shown in the specification, are disclosed. These polypeptides are novel and have natriuretic and hypotensive actions.

Abstract: A novel peptide that exhibits a natriuretic action and a vasodepressor activity, and hence, that is applicable as a diagnostic reagent. The novel peptide is manufactured by the procedure of genetic engineering as well as by the methods of purification from chicken brains or by chemical synthesis.

Abstract: A novel peptide that exhibits a natriuretic action and a vasodepressor activity, and hence, that is applicable for a diagnostic reagent. The novel peptide is manufactured by tile procedure of genetic engineering as well as by the methods of purification from frog brains or by chemical synthesis.

Abstract: Disclosed is a DNA fragment comprising a base sequence coding for a peptide occurring in human atrium cordis and having diuretic action or a precursor of the peptide, plasmids containing the DNA fragment, microorganisms transformed with the plasmid, and a process for production of the peptide using the transformant.Also disclosed is a new peptide consisting of 126 amino acids occurring in human atrium cordis and a precursor thereof. The peptide has notable diuretic action and hypotensive or antihypertensive actions.

Abstract: C-terminal .alpha.-amidating enzyme preparations, including preparations AE-I, AE-II, AE-IIa and AE-IIb, from the skin of Xenopus laevis, wherein all components can convert a peptide having a glycine residue at its C-terminal to a C-terminal amidated peptide lacking the glycine residue, and have a common N-terminal amino acid sequence represented by Ser-Leu-Ser---, and AE-I and AE-IIa have a molecular weight of about 39,000, AE-IIb has a molecular weight of about 34,000, and AE-II comprises two components having molecular weight of about 39,000 and 34,000; a process for production of the above-mentioned enzyme preparations; and a process for .alpha.-amidation of a peptide by using the above mentioned enzyme preparations.

Abstract: Disclosed herein is a physiologically-active peptide represented by the following general formula (I): ##STR1## wherein X means H or H-Asp-Ser-Gly- and Y denotes -Asn-Val-Leu-Arg-Arg-Tyr-OH, -Asn-Val-Leu-Arg-Arg-OH, -Asn-Val-Leu-Arg-Tyr-OH, -Asn-Val-Leu-Arg-OH, -Asn-Val-Leu-OH or -Asn-Ser-Phe-Arg-Tyr-OH, or a salt thereof.

Abstract: There are disclosed a new peptide .alpha.-hANP of the following structure: ##STR1## and acid addition salt thereof; a diuretic composition and a hypotensor composition containing the .alpha.-hANP or an acid addition salt thereof; and processes for the production thereof.

Abstract: Disclosed is a new protease having the following properties: (1) it is able to hydrolitically cleave a peptide bond between two adjacent basic amino acids in a peptide chain; (2) it has a molecular weight of about 43,000 as determined by electrophoresis; (3) it is inhibited by phenylmethylsulphonyl fluoride and diisopropyl fluorophosphate, but is not inhibited by monoiodoacetate, p-chloromercuribenzoic acid, ethylenediaminetetraacetic acid, 1,10-phenanthroline, tosyl-L-lysine chloromethyl ketone, and leupeptin. The protese can be produced by culturing Saccharomyces cerevisiae, and recovering purification by conventional methods, and is useful as a processing enzyme for conversion of a prohormone to an active hormone.

Abstract: There are disclosed a new peptide .beta.-rANP of the following structure: ##STR1## and acid addition salt thereof; a diuretic composition and a hypotensor composition containing the .beta.-rANP or an acid addition salt thereof; and processes for the production thereof.

Abstract: There are disclosed a new peptide .beta.-hANP of the following structure: ##STR1## and acid addition salt thereof; a diuretic composition and a hypotensor composition containing a .beta.-hANP or an acid addition salt thereof; and processes for the production thereof.

Abstract: Disclosed is a new protease having the following properties: (1) it is able to hydrolitically cleave a peptide bond between two adjacent basic amino acids in a peptide chain; (2) it has a molecular weight of about 43,000 as determined by electrophoresis; (3) it is inhibited by phenylmethylsulphonyl fluoride and diisopropyl fluorophosphate, but is not inhibited by monoiodoacetate, p-chloromercuribenzoic acid, ethylenediaminetetraacetic acid, 1,10-phenanthroline, tosyl-L-lysine chloromethyl ketone, and leupeptin. The protease can be produced by culturing Saccharomyces cerevisiae, and recovering purification by conventional methods, and is useful as a processing enzyme for conversion of a prohormone to an active hormone.