Provided is a method for measuring pentosidine in a specimen, the measurement method comprising the steps of: degrading the specimen with an amino acid degrading enzyme; contacting the specimen after the degradation step with a protein having activity that oxidatively degrades pentosidine; and detecting change resulting from the contact, wherein the amino acid degrading enzyme and the protein having activity that oxidatively degrades pentosidine are different from each other.

Provided is a method for measuring pentosidine in a specimen, the measurement method comprising the steps of: degrading the specimen with an amino acid degrading enzyme; contacting the specimen after the degradation step with a protein having activity that oxidatively degrades pentosidine; and detecting change resulting from the contact, wherein the amino acid degrading enzyme and the protein having activity that oxidatively degrades pentosidine are different from each other.

The invention relates to methods to determine KDM1A target engagement and chemoprobes useful therefor. In particular, the invention relates to non-peptidic KDM1A chemoprobes carrying a tag or label that can be used to assess KDM1A target engagement in cells and tissues. These chemoprobes can also be used to identify KDM1A interacting factors and analyze expression levels of KDM1A.

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The invention relates to methods to determine KDM1A target engagement and chemoprobes useful therefor. In particular, the invention relates to non-peptidic KDM1A chemoprobes carrying a tag or label that can be used to assess KDM1A target engagement in cells and tissues. These chemoprobes can also be used to identify KDM1A interacting factors and analyze expression levels of KDM1A.

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A biological toxicity test method for evaluating an ecological safety of an advanced oxidation process comprising the following steps: (1) collecting (preparing) a waste water to be determined; (2) collecting the waste water and a tap water after the advanced oxidation process treatment; (3) subjecting Koi (Cyprinus carpio haematopterus) to the water after treatment for exposure to poison; (4) Determining an anti-oxidation enzyme activity of a liver of the Koi after exposure; (5) Data analyzing. By comparing the changes of liver enzyme activities in different water, the present method evaluates the toxicity changes of micro-pollutant containing water before and after treatment, which fills in the gap of the ecological risk assessment for advanced oxidation technology.

A biological toxicity test method for evaluating an ecological safety of an advanced oxidation process comprising the following steps: (1) collecting (preparing) a waste water to be determined; (2) collecting the waste water and a tap water after the advanced oxidation process treatment; (3) subjecting Koi (Cyprinus carpio haematopterus) to the water after treatment for exposure to poison; (4) Determining an anti-oxidation enzyme activity of a liver of the Koi after exposure; (5) Data analyzing. By comparing the changes of liver enzyme activities in different water, the present method evaluates the toxicity changes of micro-pollutant containing water before and after treatment, which fills in the gap of the ecological risk assessment for advanced oxidation technology.

A kit used for fractionation of small dense LDL cholesterol (sdLDL-C) in a sample, including: a first reagent composition having one or two or more activities selected from the group consisting of cholesterol esterase activity, cholesterol oxidase activity, and sphingomyelinase activity; and a second reagent composition for quantifying the sdLDL-C, in which in an absorption spectrum after storing the first reagent composition at 37° C. for 2 weeks, a ratio R1 represented by ABS400/ABS450 is 0.90 or more and 3.00 or less, and in an absorption spectrum after storing the second reagent composition at 37° C. for 2 weeks, a ratio R1 represented by ABS400/ABS450 is 0.90 or more and 8.00 or less.

A reagent kit comprising a first polypeptide including a part in any one of amino acid sequences (A) to (C), and a second polypeptide including a part in any one of amino acid sequences (A) to (C), which are consistent of different sequences from a sequence of the first polypeptide; (A) an amino acid sequence in SEQ ID NO: 1 with deletion of an amino acid sequence from position 1 to 69 and an amino acid sequence from position 204 to 221, (B) an amino acid sequence in SEQ ID NO: 1 with deletion of an amino acid sequence from position 1 to 69 and deletion or substitution of at least one of amino acid residues at positions 146 to 156, (C) the amino acid sequence (A) or (B) with further deletion of at least one of amino acid residues at positions 70 to 74.

A reagent kit comprising a first polypeptide including a part in any one of amino acid sequences (A) to (C), and a second polypeptide including a part in any one of amino acid sequences (A) to (C), which are consistent of different sequences from a sequence of the first polypeptide; (A) an amino acid sequence in SEQ ID NO: 1 with deletion of an amino acid sequence from position 1 to 69 and an amino acid sequence from position 204 to 221, (B) an amino acid sequence in SEQ ID NO: 1 with deletion of an amino acid sequence from position 1 to 69 and deletion or substitution of at least one of amino acid residues at positions 146 to 156, (C) the amino acid sequence (A) or (B) with further deletion of at least one of amino acid residues at positions 70 to 74.

The present disclosure relates to an in vivo fluorescent or radioactive probe represented by a compound of formula I which is capable of longitudinal imaging of inducible nitric oxide synthase (iNOS) expression in living cells and living animals on a real time basis. The probe of the present disclosure can exhibit specific and high affinity binding to the iNOS enzyme with reduced enzyme inhibitory property and also enables longitudinal monitoring of iNOS expression along with its activity or NO production in a same experimental subject throughout the progression of a physiological or disease process without employing separate subjects as controls and experimental. The present disclosure further provides a rapid and inexpensive real time method for visualizing iNOS expression and its activity in living cells and living animals precisely, conveniently and reversibly along with simultaneous in vivo imaging of its catalytic product, nitric oxide (NO) in live physiological settings.