Abstract: A peptide has any one of the sequences SEQ ID NO.1 to SEQ ID NO.8, or has a sequence derived from any one of the sequences SEQ ID NO.1 to SEQ ID NO.8 by substitution, deletion or addition of one or several amino acids therein and having an osteogenetic activity.

Abstract: A peptide has any one of the sequences SEQ ID NO.1 to SEQ ID NO.8, or has a sequence derived from any one of the sequences SEQ ID NO.1 to SEQ ID NO.8 by substitution, deletion or addition of one or several amino acids therein and having an osteogenetic activity.

Abstract: A peptide has any one of the sequences SEQ ID NO.1 to SEQ ID NO.8, or has a sequence derived from any one of the sequences SEQ ID NO.1 to SEQ ID NO.8 by substitution, deletion or addition of one or several amino acids therein and having an osteogenetic activity.

Abstract: A peptide component (A) represented by the following formula (1a) with a peptide component (B) represented by the following formula (2a) and a compound (C) represented by the following formula (3a), as an optional component are subjected to a condensation reaction in the presence of a dehydrating and condensing agent and a condensing auxiliary; provided that in the case where “X” represents HOOC—(CH2)m—CO— in the formula (1a) and/or (2a), the reaction is conducted with the compound (C). The ratio of the peptide component (A) relative to the peptide component (B) is 100/0 to 30/70 (mol %), and the ratio of the compound (C) relative to the total molar amount of the peptide component (A) and/or the peptide component (B).

Abstract: A peptide has at least an amino acid sequence represented by SEQ ID NO:1 and it has an osteogenetic activity.

Abstract: A polyvinyl alcohol is provided containing structural units of the following formula (I) at a molar fraction of 0.05-0.50 and the structural units of the following formula (II) at a molar fraction of 0.0001 to 0.50; ##STR1## wherein R.sup.1, R.sup.2, R.sub.3 and X are as desribed herein, and its use in preparation of gels, particularly hydrogels, effective for use in wound dressing materials.

Abstract: Provided is a medical material useful for wound dressings or a drug delivery system, which material is safe and has high healing effects, more specifically, which is free from cytotoxicity or other side effects caused by a drug and permits the selective healing of the diseased site in a small dosage without damaging the sites other than the diseased site.The medical material so provided is a polymer gel having a sequence represented by the formula: A-Sp1-E-Sp2-G wherein A represents a water-swelling polymer gel, Sp1 represents the first spacer, E represents a cleavable group with the main chain to be cleaved via an enzymatic reaction, Sp2 represents the second spacer and G represents a drug. When the polymer gel is used, the cleavable group (E) is cleaved according to an amount of an enzyme existing at the diseased site to release the drug in accordance with the amount of the enzyme.

Abstract: A polyvinyl alcohol is provided containing structural units of the following formula (I) at a molar fraction of 0.05-0.50 and the structural units of the following formula (II) at a molar fraction of 0.0001 to 0.50; ##STR1## wherein R.sup.1, R.sup.2, R.sup.3 and X are as desribed herein, and its use in preparation of gels, particularly hydrogels, effective for use in wound dressing materials.

Abstract: A medical polymer gel produced by immobilizing a drug onto a water swelling polymer gel through a cleavable group with the main chain to be cleaved via an enzymatic reaction and a spacer, and a water swelling polymer gel produced by covalently crosslinking a polysaccharide having a carboxyl group within the molecule with a diaminoalkane derivative as the crosslinking reagent. Because the medical polymer gel exerts a drug releasing property depending on the level of an enzyme, the gel can release a therapeutically effective dose of a drug only at a focal lesion generating the enzyme. The medical polymer gel is useful as the structural component of wound dressings, adhesives for biological tissues, adhesion preventing agents, bone reinforcing agents, and drug releasing base materials. Wound dressings comprising the structural material of the water swelling polymer gel of the present invention, can be applied to a patient with wound, burn, and decubitus to promote the healing of the wounds of the patient.

Abstract: The present invention provides a wound dressing composed of a hydrogel with the principal component being a vinyl alcohol polymer of a viscosity average polymerization degree of 300 or more, wherein the vinyl alcohol polymer contains 5 to 50 mol % of one or more vinyl ester units represented by the following formula (I): ##STR1## and the vinyl alcohol polymer has a block character (.eta.) of 0.6 or less, the block character being represented by the following mathematical formula (II);.eta.=?OH, VES!/2?OH!?VES! (II)Because the wound dressing of the present invention is excellent in terms of transparency, flexibility, hot water resistance, water absorption, and safety, the dressing is useful for the treatment and promotion of the healing of wounds including general wounds such as abrasions, cuts and acne; surgery wounds such as excision wounds and dermabrasions; burns; ulcers; and pressure sores.

Abstract: A water swelling polymer gel produced by covalently crosslinking a polysaccharide having a carboxyl group within the molecule with a diaminoalkane derivative as the crosslinking reagent. The medical polymer gel is useful as the structural component of wound dressings, adhesives for biological tissues, adhesion preventing agents, bone reinforcing agents, and drug releasing base materials. Wound dressings comprising the structural material of the water swelling polymer gel of the present invention, can be applied to a patient with wound, burn, and decubitus to promote the healing of the wounds of the patient.

Abstract: Peptides having high binding activity for human interleukin-1 and represented by the following formulaH-X.sup.1 -Cys-A-B-A-B-A-Ser-X.sup.2 -Ywherein each A represents an amino acid residue selected from the group consisting of Val, Leu, Ile and Nle, independent of any other selection for A; B represents an amino acid residue selected from the group consisting of Arg, Lys, Gln, His and Ser, independent of any other selection for B; X.sup.1 and X.sup.2 each is a single bond or a peptide segment comprising 1-10 amino acid residues selected from Gly, Ala, Val, Arg, Asn, Ser, Phe, Pro, Leu, Glu, Asp, Lys, Thr, His, Tyr, Nle and Ile and Y represents a hydroxyl group or an amino group; and their salts.

Abstract: A human IgG.sub.1 type monoclonal antibody which possesses a molecular weight in the range of 180,000.+-.20,000 as measured by the method of polyacrylamide gel electrophoresis performed in the presence of sodium dodecyl sulfate and is specific to nicotinic acetylcholine receptor. The human IgG.sub.1 type monoclonal antibody mentioned above is produced by a method which comprises fusing human cells capable of producing an antibody against nicotinic acetylcholine receptor with propagable human cells thereby giving rise to a hybridoma capable of producing the aforementioned human IgG.sub.1 type monoclonal antibody, selecting the hybridoma from the production of the fusion, culturing the hybridoma thereby giving rise to the aforementioned human IgG.sub.1 type monoclonal antibody, and selecting the antibody from the cultured medium. The hybridoma mentioned above is also identified.

Abstract: A peptide being capable of binding to interleukin 6, and an adsorbent for interleukin 6 comprising the peptide immobilized on a carrier.

Abstract: There is disclosed an adsorbent, comprising a carrier on which is immobilized a peptide possessing an ability to bind to the human antibody to the nicotinic acetylcholine receptor and represented by the formula:H--X--A--Y--Zwherein A stands for a peptide residue, one of X and Y stands for a single bond, an amino acid residue selected from the class consisting of Asp, Glu, Lys and a divalent group represented by the formula, ##STR1## (wherein n stands for an integer in the range of 1 to 17), or a peptide residue formed by peptide linkage of two to ten amino acid residues of at least one species selected from the class mentioned above and the other of X and Y stands for an amino acid residue selected from the class consisting of Asp, Glu, Lys and a divalent group represented by the formula, ##STR2## (wherein n stands for an integer in the range of 1 to 17), or a peptide residue formed by peptide linkage of two to ten amino acid residues of at least one species selected from the class mentioned above and Z stand

Abstract: A monoclonal anti-idiotypic antibody specific to a human IgG.sub.1 type monoclonal antibody possessing specificity to nicotinic acetylcholine receptor; a method for the production of the aforementioned monoclonal anti-idiotypic antibody by the steps of immunizing an animal with a human IgG.sub.1 type monoclonal antibody specific to nicotinic acetylcholine receptor, collecting antibody-producing cells from the animal, fusing the collected cells with neoplastic cells, selecting from the product of fusion a hybridoma capable of producing a monoclonal anti-idiotypic antibody specific to the human IgG.sub.1 type monoclonal antibody possessing specificity to nicotinic acetylcholine receptor, propagating the selected hybridoma thereby giving rise to said monoclonal anti-idiotypic antibody, and collecting the produced monoclonal anti-idiotypic antibody; and use of the monoclonal anti-idiotypic antibody as a reagent and as an adsorbent.

Abstract: A monoclonal antibody specific for an .alpha..sub.1 -acid glycoprotein or for at least one antigenic determinant included in a sugar chain of the following formula: ##STR1## wherein Gal means galactose, GlcNAc means N-acetylglucosamine, Man means mannose, Fuc means fucose, and n is 0 or 1, which is useful for the measurement of glycoproteins in cells, tissues and blood and therefore is useful for diagnosis of various diseases, particularly tumors, and a method for the production thereof by fusing a neoplasm cell line with antibody-producing cells from an animal which has been immunized against an desialylated glycoprotein and culturing the resultant hybridoma.

Abstract: A peptide is disclosed which is represented by the formula:H-X-Gly-Trp-Lys-His-Trp-Val-Tyr-Tyr-Thr-Cys-Cys-Pro-Asp-Thr-Pro-Tyr-Leu-Asp -Y -Zwherein one of X and Y stands for a single bond, an amino acid residue selected from the class consisting of Asp, Glu, Lys and a divalent group represented by the formula, ##STR1## (wherein n stands for an integer in the range of 1 to 17), or a peptide residue formed by peptide linkage of two to ten amino acid residues of at least one species selected from the class mentioned above, the other of X and Y stands for an amino acid residue selected from the class consisting of Asp, Glu, Lys and a divalent group represented by the formula, ##STR2## (wherein n stands for an integer in the range of 1 to 17), or a peptide residue formed by peptide linkage of two to ten amino acid residues of at least one species selected from the class mentioned above and Z stands for a hydroxyl group or an amino group, and two cysteinyl mercapto groups in the Cys-Cys moiety may be interlinked to

Abstract: Treatment of the blood by means of a blood purification device comprising packed, substantially spherical, smooth-surfaced, porous granules having at least 0.1 .mu.mole/m.sup.2 of the silanol group on the surface thereof, a blood inlet and a blood outlet scarcely causes decrease in leukocyte or platelet count or blood cell damage and can remove proteins from the blood by adsorption without high pressure loss.

Abstract: Treatment of the blood by means of a blood purification device comprising packed, substantially spherical, smooth-surfaced, porous granules having at least 0.1 .mu.mole/m.sup.2 of the silanol group on the surface thereof, a blood inlet and a blood outlet scarcely causes decrease in leukocyte or platelet count or blood cell damage and can remove proteins from the blood by adsorption without high pressure loss.