Abstract: A highly sensitive quantitative assay method for any one component which is L-glycero-3-phosphate (G3P), dihydroxyacetone-3-phosphate (DHAP), nicotinamide adenine dinucleotide (NAD) or reduced NAD, in a specimen to be assayed, comprising causing this component in the specimen to take part in the cycling reaction ##STR1## wherein GPO is glycerophosphate oxidase and GPDH is glycerophosphate dehydrogenase, and measuring a detectable change in the reaction system. There is thus provided a novel G3P-GHAP cycling reaction using GPO, which consumes O.sub.2 and generates H.sub.2 O.sub.2 and DHAP, with a substrate of G3P, and furthermore GPDH which consumes reduced NAD and generates NAD and G3P, with a substrate of DHAP. Examples of specimens are specimens which contain any one of G3P, DHAP, NAD or reduced NAD, or which liberate or generate such a component.

Abstract: An enzyme which acts on a reducing terminal of a monosaccharide or oligosaccharide without requiring NAD or NADP and which catalyzes the reaction ##STR1## wherein R is a saccharide chain residue or hydrogen, A is a hydrogen acceptor other than NAD or NADP, AH or AHn is a reduced form acceptor and n is 1 or 2. This maltose dehydrogenase is produced by culturing a microorganism belonging to genus Staphylococcus, specifically, sp. B-0875 FERM BP-385, and isolating the thus-produced maltose dehydrogenase from the culture medium. An assay method for the determination of saccharide or the activity of a saccharide liberating enzyme, comprises reacting this enzyme with a substrate in the presence of a hydrogen acceptor, and measuring the amount of a detectable change.

Abstract: A method for assaying a compound of the formula ##STR1## wherein R.sub.1 is hydroxyl or amino, or hydrogen if at least one of R.sub.2, R.sub.3, R.sub.4, R.sub.5 and R.sub.6 is hydroxyl or amino, and R.sub.2, R.sub.3, R.sub.4, R.sub.5 and R.sub.6 are hydrogen, halogen, lower alkyl, lower alkoxy, amino, substituted amino, hydroxy, carboxyl or sulfo, or R.sub.5 and R.sub.6 together form a ring, comprises establishing a reaction system containing the compound to be assayed and a coupler and an enzyme capable of consuming oxygen and generating a pigment in the presence of the compound and the coupler. A detectable change in the reaction system is measured, to assay the compound in question. The measurement can comprise the measurement of consumed oxygen, as by an oxygen electrode. Or the measurement can comprise the measurement of the generated pigment, as by a colorimetric assay at a specific absorption wavelength thereof.

Abstract: A method for assay of enzyme activity which comprises treating an amide compound of the formula ##STR1## with peptidase; treating thus-liberated amine of the formula ##STR2## with an oxidase which consume oxygen and forms pigment by oxidative condensation of said amine with a coupler of the formula ##STR3## and quantitatively measuring the detectable changes. Also disclosed is an assay method which comprises treating an amide compound of the formula ##STR4## or a salt thereof, with peptidase to liberate an aniline derivative of the formula ##STR5## oxidizing said aniline derivative; and quantitatively measuring detectable change.

Abstract: Compounds of the formula ##STR1## wherein R.sub.1 is lower alkyl, lower alkoxycarbonyl-lower alkyl, phenyl, phenyl substituted by one or more lower alkyl or halogen, phenyl-lower alkyl optionally substituted in its side chain by lower alkyl or lower alkoxycarbonyl, thienylmethyl or thiazolyl, R.sub.2 is hydrogen or lower alkyl, or ##STR2## constitutes a 3-7-membered nitrogen-containing heterocyclic ring in which R.sub.1 and R.sub.2 are connected, R.sub.3 is hydrogen or hydroxyl, and X is oxygen or sulfur, or a non-toxic salt thereof. These compounds have stronger antibacterial activity as compared with known clinically used macrolide antibiotics such as erythromycin, oleandomycin, josamycin and leucomycin, and also have strong antibacterial activity against all macrolide antibiotic-resistant strains such as macrolide-resistant A group strains (clinical isolates or erythromycin, oleandomycin and 16-membered macrolide antibiotic resistant strains).

Abstract: A peptide of the formula ##STR1## wherein A is Tyr or Phe, or a pharmaceutically acceptable salt thereof, is useful for the diagnosis of parathyroid gland function. When A is Tyr, the peptide can be labelled with iodine-125 without losing its PTH activity and without undergoing oxidation upon storage.

Abstract: Novel 3-O-acyl-4"-deoxydesmycosin derivatives of the formula ##STR1## wherein R.sub.1 is lower alkyl, phenyl, substituted phenyl, phenyl-lower alkyl or substituted phenyl-lower alkyl, R.sub.2 is hydrogen or --CHO and R.sub.3 is hydrogen or hydroxyl, or a non-toxic salt thereof, can be produced by acylating the hydroxyl group at position-3 of the corresponding intermediate while protecting the hydroxyl at position-2' or positions-2' and -4' with acetyl, and then removing the protective group or groups. These derivatives have antibiotic utility against Gram positive and Gram negative bacteria.

Abstract: Compounds of the formula wherein R is ##STR1## in which R.sub.1, R.sub.2 and R.sub.3 are the same or different and are selected from the group consisting of hydrogen, chlorine, bromine, lower alkyl, lower alkoxy and naphthyl, provided that when R.sub.1 is lower alkyl, R.sub.2 and R.sub.3 are hydrogen, chlorine, bromine or lower alkoxy, or a pharmaceutically acceptable salt thereof, have anti-carrageenin edema activity, and are useful as anti-inflammatory agents and immuno modulators. They are produced by reacting an amide of the formula ##STR2## wherein R has the same meanings hereinabove, with N,N'-ethylene thiourea.

Abstract: Neplanocin A derivatives of the formula ##STR1## wherein R.sub.1 and R.sub.2 are hydrogen or benzoyl, R.sub.3 is hydrogen or OR.sub.8, R.sub.5 is hydrogen or acetyl, R.sub.6 is hydrogen, acetyl or benzoyl, when R.sub.3 is hydrogen, R.sub.4 is hydrogen or halogen, hydroxy, acetoxy, acetylthio, amino or azide, and when R.sub.3 is OR.sub.8, R.sub.4 is hydrogen, R.sub.8 is hydrogen or acetyl, or R.sub.8 and R.sub.5 together form benzylidene, and at least one of R.sub.8, R.sub.5 and R.sub.6 is other than hydrogen. The compounds of the present invention have inhibitory action for the growth of L 5178 Y cells and have the same or superior activity as neplanocin A, and hence are useful as antitumor agents.

Abstract: L-glutamic acid oxidase having the following biochemical properties:(a) substrate specificity: L-glutamic acid,(b) enzyme action: catalyzes a reaction which forms one mole of .alpha.-ketoglutaric acid, one mole of ammonia and one mole of hydrogen peroxide from one mole of L-glutamic acid, one mole of oxygen and one mole of water, as follows: ##STR1## This oxidase is produced by culturing microorganisms belonging to genus Streptomyces in a nutrient medium and isolating the thus-produced L-glutamic acid oxidase. Particular microorganisms of genus Streptomyces are sp. A7700 FERM P-6241 (NRRL No. 15267) and sp. 8063 FERM P-6242 (NRRL No. 15268). The oxidase can be used for detecting L-glutamic acid or L-glutamate, in an aqueous sample, because it catalyzes a reaction which forms one mole of .alpha.-ketoglutaric acid, one mole of ammonia and one mole of hydrogen peroxide from one mole of glutamic acid, one mole of oxygen and one mole of water.

Abstract: A compound of the formula ##STR1## wherein R is L-leucyl or .gamma.-L-glutamyl and X and Y are halogen and are the same or different, or a salt thereof. These compounds are useful as synthetic substrates for assaying peptidase activity.

Abstract: A compound of the formula ##STR1## wherein R.sub.1 is hydrogen, --COOR.sub.11 or ##STR2## R.sub.11 is optionally substituted lower alkyl, R.sub.12 is optionally substituted hydrocarbon, heterocyclic or heterocyclic-lower alkyl, R.sub.13 is hydrogen or lower alkyl, or R.sub.12 and R.sub.13 together constitute a heterocyclic ring together with the attached nitrogen atom, and R.sub.2 is hydrogen or hydroxyl, or a pharmaceutically-acceptable salt thereof, has stronger antibacterial activity against Gram-positive bacteria than does tylosin. It is produced by deformylation, or by oxidizing a formyl at position-14, or by amidating the latter compound.

Abstract: A new synthesis of 5-deazariboflavine is afforded by condensing N-D-ribityl-3,4-xylidine with a novel chemical intermediate, 6-chloro-5-formyluracil.

Abstract: A high sensitivity assay method of the coenzyme cyclic assay type, eliminates the need for a separate indication reaction, by using the cycling reaction itself as the indication reaction, according to the following steps: ##STR1## the thus-formed formazan is then colorimetrically measured, to give a highly sensitive determination of the quantity of the substance to be assayed, e.g. NAD.sup.+, NADP.sup.+, malic acid or .gamma.-aminobutyric acid in human serum.

Abstract: Compounds of the formula ##STR1## wherein R is ##STR2## in which R.sub.1, R.sub.2 and R.sub.3 are the same or different and are selected from the group consisting of hydrogen, chlorine, bromine, lower alkyl, lower alkoxy and naphthyl, provided that when R.sub.1 is lower alkyl, R.sub.2 and R.sub.3 are hydrogen, chlorine, bromine or lower alkoxy, or a pharmaceutically acceptable salt thereof, have anti-carrageenin edema activity, and are useful as anti-inflammatory agents and immuno modulators. They are produced by reacting an amide of the formula ##STR3## wherein R has the same meanings hereinabove, with N,N'-ethylene thiourea.

Abstract: Antibiotic acmimycin of the formula ##STR1## is active against Gram positive and Gram negative bacteria. It is produced by culturing the microorganism Streptomyces sp. AC4559 FERM P-6445, and isolating the above compound from the cultured medium.

Abstract: Novel 23-demycinosyldesmycosin derivatives are disclosed of the formula ##STR1## wherein A is oxygen or sulfur, R.sub.1 is optionally substituted phenyl or ##STR2## group, in which R.sub.3 is optionally substituted phenyl and R.sub.4 and R.sub.5 are the same or different and are hydrogen, lower alkyl or optionally substituted phenyl, and R.sub.2 is hydrogen or hydroxyl. The compounds or non-toxic salts thereof are useful as antibiotics.

Abstract: Tyramine oxidase, which is useful for the clinical diagnosis of leucine aminopeptidase activity in serum, is produced by culturing the microorganism Arthrobacter sp. B-0813 FERM-P No. 6240 in a nutrient medium, and isolating thus-produced tyramine oxidase from the cultured medium.

Abstract: Apparatus for performing an immunoassay, comprises in combination a reaction tube closed at its bottom, and in the reaction tube a molded element having on its surface material having specific binding ability for a component in a liquid specimen to be assayed. The shape of the surface of the element adjacent the interior surface of the tube is the complement of the shape of the interior surface of the tube. A spacer rib is provided on the element, in contact with the interior surface of the tube. This rib holds the element in such position in the tube that the surfaces of complementary shape of the element and tube are shaped from each other a small but constant distance. A thin layer of constant thickness of a liquid specimen for immunoassay is thus receivable between the complementary surfaces. This arrangement increases the contact surface of the liquid medium in the reaction tube by the element, by establishing a homogeneous uniform layer of liquid medium.

Abstract: An enzyme having enoyl-CoA hydratase activity, 3-hydroxyacyl-CoA dehydrogenase activity and 3-ketoacyl-CoA thiolase activity, all in the same enzyme, is produced by culturing the microorganism strain Pseudomonas fragi B-0771 FERM-P No. 5701, and isolating the enzyme thus produced from the culture medium. Such an enzyme is useful in an assay method for a fatty acid component in a sample, which fatty acid is originally present in the sample or is liberated from a fatty acid ester in the sample, comprising:(a) converting the fatty acid to acyl-CoA;(b) converting the thus-produced acyl-CoA to dehydroacyl-CoA;(c) converting the thus-produced dehydroacyl-CoA to hydroxyacyl-CoA;(d) converting the thus-produced hydroxyacyl-CoA to ketoacyl-CoA;(e) converting the thus-produced ketoacyl-CoA to acyl-CoA; and measuring the detectable changes in the reaction mixture.