Toyo Jozo Kabushiki Kaisha

Toyo Jozo Company, Ltd.

Kokusan Chemical Works Limited

Kunio Matsumoto

Susumu Watanabe

Tsutomu Hirata

Tadashiro Fujii

Akira Ohtsuka

Yoshitaka Kagimoto

Rokuro Izumi

Hideji Seijo

Hiroyuki Mizuguchi

Kiyoharu Takahashi

Masataka Morishita

Masaki Takada

Toshiharu Noda

Mitsuru Fukushima

Tetsuo Matsuda

Shigeo Katsuragi

Kazuhiko Matsumoto

Tsutomu Yamaguchi

Yuzo Shibuya

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.

Enzymatic assay method

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.

Assaying peptidase enzyme activity

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.

Novel synthetic substrate and assay method using the same

Acrylonitrile polymer containing amino groups and having a porous structure containing micro-pores with an average size of from 50 to 2000 .ANG. and pore volume of not less than 0.2 cm.sup.3 /g is prepared by reducing an acrylonitrile polymer having said porous structure in an inert non-solvent for said polymer with lithium aluminum hydride. The polymer obtained is useful as a carrier for enzymes.

Process for preparing an amino group-containing polyacrylonitrile polymer

A process for the production of amine oxidase, which comprises culturing an amine-oxidase-producing microorganism belonging to the genus Talaromyces, genus Eupenicillium, genus Petromyces, genus Neosartorya or genus Eurotium, and isolating the thus-prepared amine oxidase from the cultured medium. The preferred strains of microorganisms under these genera are Talaromyces flavus var. flavus M 4175 FERM-P No. 5866, Eupenicillium parvum M 5051 FERM-P No. 5870, Petromyces alliaceus M 4648 FERM-P No. 5867, Neosaytorya fischeri M 4690 FERM-P No. 5868 and Eurotium chevalieri M 4805 FERM-P No. 5869.

Process for the production of amine oxidase

Novel amine compounds of the formula ##STR1## wherein R.sub.1 is lower alkyl and R.sub.2 is substituted methyl amino or D-amino acid residue, or a salt thereof. R.sub.1 can typically be isobutyl or methyl; and R.sub.2 can be methylamino of the formula

Assay method of enzyme activity

Biological material such as enzymes is immobilized by adsorption or covalent bonding to a micro-porous water-insoluble acrylonitrile polymer containing from 20 .mu.M to 1000 .mu.M of amino groups per gram of the polymer. Covalent bonding may be carried out with a crosslinking or condensing agent. The amino groups may be introduced into the polymer by reduction of nitrile groups with lithium aluminum hydride in an inert non-solvent.

Immobilization of biological material with an acrylonitrile polymer

7-Amino-cephem compounds are produced from 7-substituted-cephem compounds by the enzymatic action of microorganisms Comamonas sp. SY-77-1 FERM-P 2410 or Pseudomonas ovalis ATCC 950.

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Mishima, Japan

Kunio Matsumoto