A mutant-type uricase, PEG modified mutant-type uricase, and application thereof. The mutant-type uricase has a cysteine residue introduced by recombination, the cysteine residue is located at an inactive region of the uricase, and one or more PEGs are coupled to the mutant-type uricase. The resulting PEGylated mutant-type uricase has characteristics of a half-life extension, product uniformity, and stable enzyme activity. Therefore, the present invention has a wide future application range.

A mutant-type uricase, PEG modified mutant-type uricase, and application thereof. The mutant-type uricase has a cysteine residue introduced by recombination, the cysteine residue is located at an inactive region of the uricase, and one or more PEGs are coupled to the mutant-type uricase. The resulting PEGylated mutant-type uricase has characteristics of a half-life extension, product uniformity, and stable enzyme activity. Therefore, the present invention has a wide future application range.

A disposable sensor chip for biological component concentration measurement includes: a chip main body defining a cavity through which a body fluid is flowable; and a reagent located in the cavity such that the body fluid flowing through the cavity comes into contact with the reagent. The reagent comprises a 2-substituted benzothiazolyl-3-substituted phenyl-5-substituted sulfonated phenyl-2H-tetrazolium salt.

A disposable sensor chip for biological component concentration measurement includes: a chip main body defining a cavity through which a body fluid is flowable; and a reagent located in the cavity such that the body fluid flowing through the cavity comes into contact with the reagent. The reagent comprises a 2-substituted benzothiazolyl-3-substituted phenyl-5-substituted sulfonated phenyl-2H-tetrazolium salt.

A 2-substituted benzothiazolyl-3-substituted phenyl-5-substituted sulfonated phenyl-2H-tetrazolium salt represented by the following Formula (1): ##STR00001##
wherein, R.sup.1 can be a hydrogen atom, a hydroxyl group, a methoxy group, and an ethoxy group; R.sup.2 can be a nitro group, OR.sup.4, and a carboxyl group; R.sup.3 is a hydrogen atom, a methyl group, or an ethyl group, while at least one is a methyl group or an ethyl group; R.sup.4 is a methyl group or an ethyl group; m is 1 or 2; n is an integer from 0 to 2; p is 0 or 1; n+p is 1 or greater; q is 1 or 2; when q is 2, the OR.sup.3's are disposed adjacently to each other and may form a ring; and X is a hydrogen atom or an alkali metal atom.

A 2-substituted benzothiazolyl-3-substituted phenyl-5-substituted sulfonated phenyl-2H-tetrazolium salt represented by the following Formula (1): ##STR00001##
wherein, R.sup.1 can be a hydrogen atom, a hydroxyl group, a methoxy group, and an ethoxy group; R.sup.2 can be a nitro group, OR.sup.4, and a carboxyl group; R.sup.3 is a hydrogen atom, a methyl group, or an ethyl group, while at least one is a methyl group or an ethyl group; R.sup.4 is a methyl group or an ethyl group; m is 1 or 2; n is an integer from 0 to 2; p is 0 or 1; n+p is 1 or greater; q is 1 or 2; when q is 2, the OR.sup.3's are disposed adjacently to each other and may form a ring; and X is a hydrogen atom or an alkali metal atom.

Methods and kits for predicting infusion reaction risk and antibody-mediated loss of response during intravenous PEGylated uricase therapy in gout patients is provided. Routine SUA monitoring can be used to identify patients receiving PEGylated uricase who may no longer benefit from treatment and who are at greater risk for infusion reactions.

The present invention relates, e.g., to in vitro method, using isolated protein reagents, for joining two double stranded (ds) DNA molecules of interest, wherein the distal region of the first DNA molecule and the proximal region of the second DNA molecule share a region of sequence identity, comprising contacting the two DNA molecules in a reaction mixture with (a) a non-processive 5 exonuclease; (b) a single stranded DNA binding protein (SSB) which accelerates nucleic acid annealing; (c) a non strand-displacing DNA polymerase; and (d) a ligase, under conditions effective to join the two DNA molecules to form an intact double stranded DNA molecule, in which a single copy of the region of sequence identity is retained. The method allows the joining of a number of DNA fragments, in a predetermined order and orientation, without the use of restriction enzymes.

The present invention relates, e.g., to in vitro method, using isolated protein reagents, for joining two double stranded (ds) DNA molecules of interest, wherein the distal region of the first DNA molecule and the proximal region of the second DNA molecule share a region of sequence identity, comprising contacting the two DNA molecules in a reaction mixture with (a) a non-processive 5 exonuclease; (b) a single stranded DNA binding protein (SSB) which accelerates nucleic acid annealing; (c) a non strand-displacing DNA polymerase; and (d) a ligase, under conditions effective to join the two DNA molecules to form an intact double stranded DNA molecule, in which a single copy of the region of sequence identity is retained. The method allows the joining of a number of DNA fragments, in a predetermined order and orientation, without the use of restriction enzymes.

The present invention relates, e.g., to in vitro method, using isolated protein reagents, for joining two double stranded (ds) DNA molecules of interest, wherein the distal region of the first DNA molecule and the proximal region of the second DNA molecule share a region of sequence identity, comprising contacting the two DNA molecules in a reaction mixture with (a) a non-processive 5 exonuclease; (b) a single stranded DNA binding protein (SSB) which accelerates nucleic acid annealing; (c) a non strand-displacing DNA polymerase; and (d) a ligase, under conditions effective to join the two DNA molecules to form an intact double stranded DNA molecule, in which a single copy of the region of sequence identity is retained. The method allows the joining of a number of DNA fragments, in a predetermined order and orientation, without the use of restriction enzymes.