Abstract: An injectable oil-in-water emulsion composition comprises an antifungal triazole compound of the following formula (I) ##STR1## wherein Ar represents a substituted phenyl group; R.sup.1 and R.sup.2 represent, independently, a hydrogen atom or a lower alkyl group, or R.sup.1 and R.sup.2 may together form a lower alkylene group; R.sup.4 represents a hydrogen atom or an acyl group; and A represents an optionally substituted cyclic amide group bonded through a nitrogen atom, or a salt thereof. The solubility of the triazole compound having poor water-solubility and fat-solubility can remarkably be increased by dispersing in water with use of an oil component (e.g. a triglyceride of fatty acids) and an emulsifier (e.g. a phospholipid).

Abstract: A bacterium of the genus Bacillus is transformed by introducing a vector incorporating DNA encoding an antibody; the resulting transformant is cultivated in a medium to produce and accumulate the antibody in an active form in the culture liquid. According to this method, a recombinant antibody can be easily produced in an active form in large amounts, owing to success in secretory expression using a bacterium of the genus Bacillus.

Abstract: The present invention provides a hybrid monoclonal antibody having specificities against fibrin and thrombolytic substance, a polydoma which produces said antibody and thrombolytic agent comprising said antibody and thrombolytic substance which is immunologically coupled thereto, and methods of using said antibody in combination with thrombolytic substance for lysis or removal of thrombi.

Abstract: Disclosed are a bispecific hybrid MoAb having specificity for both an activated platelet and a substance having thrombolytic activity, and a thrombolytic agent comprising the above bispecific MoAb and a substance having thrombolytic activity immunologically bound thereto, whereby efficient, rapid thrombolysis is possible.

Abstract: The present invention discloses, a bispecific monoclonal antibody to an ansamitocin derivative and a target antigen, particularly tumor-associated antigen, which can carry an ansamitocin derivative in a stable and inactive form at other sites than the target and release the active-form ansamitocin derivative at the target site, so that an anticancer agent having excellent durability and selectivity with little adverse action can be prepared using the bispecific monoclonal antibody and ansamitocin derivatives.

Abstract: Lymphotoxin (LT) mutein (genetically-altered LT) is disclosed that has the following amino acid sequence, or a portion of an active portion of said protein, where 10 to 21 amino acids of LT being deleted from N-terminus and which has Pro or Phe at the N-terminus: ##STR1## Wherein R.sub.1 is Pro or Phe, R.sub.2 is a peptide chain represented by the following sequence:Ala-Gln-Thr-Ala-Arg-Gln-His-Pro-Lys-Met-His-Leu,or a portion thereof and n is 0 or 1.The LT mutein can be recovered in a higher yield and purified more efficiently under mild conditions which does not harm the LT's biological activity, than the whole LT.

Abstract: Disclosed is a novel recombinant human lyphotoxin (LT) mutein which combines with an antibody at an inactive site of an LT molecule and liberates the LT molecule easily from the antibody after incorporation of the mutein into tumor cells.The recombinant human LT mutein is prepared by introducing a polydeoxyribonucleic acid containing a nucleotide sequence coding for the particular amino acid sequence into a replicable vector, transforming a microorganism or a cell with the recombinant DNA thus obtained, and cultivating the resulting transformant to express genetic information of the polydeoxyribonucleic acid.The recombinant human LT mutein is useful for tumor-selective carcinostatics, and effective for increasing the actively of LT and reducing the side effects thereof.

Abstract: The present invention discloses, a bispecific monoclonal antibody to an ansamitocin derivative and a target antigen, particularly tumor-associated antigen, which can carry an anasamitocin derivative in a stable and inactive form at other sites than the target and release the active-form ansamitocin derivative at the target site, so that an anticancer agent having excellent durability and selectivity with little adverse action can be prepared using the bispecific monoclonal antibody and ansamitocin derivatives.

Abstract: In an enzyme immunoassay, when a specific antibody produced by contacting a peptide essential to the formation of a specific antibody to a peptide antigen, a freeze-dried material of .beta.-D-galactosidase-enzyme conjugate or a peptide-enzyme conjugate prepared by coupling a labeling enzyme with a peptide of the general formula:H-R.sub.1 -Pro-Ser-Asp-Thr-Pro-Ile-Leu-Pro-Gln-OHwherein R.sub.1 is a peptide fragment consisting of 1 to 14 amino acid residues including Gly in the 14-position of the peptide Ala.sup.1 -Pro.sup.2 -Pro.sup.3 -Pro.sup.4 -Ser.sup.5 -Leu.sup.6 -Pro.sup.7 -Ser.sup.8 -Pro.sup.9 -Ser.sup.10 -Arg.sup.11 -Leu.sup.12 -Pro.sup.13 -Gly.sup.14 is used, a high reproducibility of the result of the enzyme immunoassay is obtained.

Abstract: In a method for immunochemical assay of human chorionic gonadotropin involving use of an antibody immobilized on a carrier, an antigen and an antibody to which a labeling agent has been attached, when the antibody supported on the carrier and the antibody coupled to a labeling agent are different antibodies which are not overlapping in antigen-determining site and one of said different antibodies is specifically reactive to human chorionic gonadotropin, a high reproducibility of the result of the immunochemical assay is obtained.

Abstract: A novel peptide-enzyme conjugate obtained by coupling a labeling enzyme with a peptide of the general formula:H-R.sub.1 -Phe-Val-Gln-Trp-Leu-R.sub.2 -Asn-Thr-OH(wherein R.sub.1 is a peptide fragment consisting of 1 to 10 amino acid residues in the sequence of and including the Asp in 10-position of ##STR1## and R.sub.2 is Met or Nle) is useful for a method for enzyme immunoassay of pancreatic glucagon.

Abstract: The non-specific inhibitors of hemagglutination in a subject serum for hemagglutination-inhibition test for a togavirus such as rubella virus can be inactivated by subjecting the subject serum to the action of phospholipase C. By subjecting thus-treated serum to the hemagglutination-inhibition test employing fixed erythrocytes the togavirus hemagglutination-inhibition antibody titer of the serum can be determined accurately and with high sensitivity.

Abstract: In the rubella virus hemagglutination-inhibition test, the hemagglutination-inhibition antibody titers of the test sera can be determined with accuracy and high sensitivity by employing a novel diluent, which contains N-2-hydroxyethylpiperazine-N'-2'-ethanesulfonic acid in a low concentration and which is free from calcium ion, for the dilution of the rubella virus hemagglutinating antigen and of the test sera.