Abstract: Disclosed are methods and reagents for the enzymatic measurement of short-chain fatty acids, having 3 to 6 carbon atoms, in a sample. Methods include the use of recombinant butyrate kinases from multiple species, combined various reagents that includes ATP, to detect butyric acid in different types of samples via measurement of ATP consumption. Disclosed also are the reagents themselves.

Abstract: Disclosed is an enzymatic measurement method comprising: contacting butyric acid in a sample, adenosine triphosphate (ATP), and butyrate kinase to produce adenosine diphosphate (ADP); and measuring the produced ADP.

Abstract: An object of the present invention is to provide a highly versatile, simple and safe method for measuring Lp-PLA2 activity. Another object of the present invention is to provide an accurate and highly sensitive method for measuring Lp-PLA2 activity. Provided is a method for measuring lipoprotein-associated phospholipase A2 (Lp-PLA2) activity in a sample containing Lp-PLA2, the method comprising the following steps (A) to (C): (A) converting PAFs into lyso-PAFs by reacting the PAFs with the Lp-PLA2 in the sample; (B) hydrolyzing the lyso-PAFs produced in the step (A) with an enzyme (lyso-PAF-PLD) to obtain hydrolysate; and (C) measuring Lp-PLA2 activity in the sample by utilizing a quantitative change attributable to the hydrolysate obtained in step (B) as an indicator.

Abstract: An object of the present invention is to provide a highly versatile, simple and safe method for measuring Lp-PLA2 activity. Another object of the present invention is to provide an accurate and highly sensitive method for measuring Lp-PLA2 activity. Provided is a method for measuring lipoprotein-associated phospholipase A2 (Lp-PLA2) activity in a sample containing Lp-PLA2, the method comprising the following steps (A) to (C): (A) converting PAFs into lyso-PAFs by reacting the PAFs with the Lp-PLA2 in the sample; (B) hydrolyzing the lyso-PAFs produced in the step (A) with an enzyme (lyso-PAF-PLD) to obtain hydrolysate; and (C) measuring Lp-PLA2 activity in the sample by utilizing a quantitative change attributable to the hydrolysate obtained in step (B) as an indicator.

Abstract: The present invention provides a measuring method for at least one of a kinase forward reaction substrate, a phosphorylated product thereof, and a precursor thereof, and includes a step of conducting an enzymatic cycling reaction by bringing at least a kinase, a first nucleotide coenzyme of the kinase, and a second nucleotide coenzyme having a different nucleoside moiety from the first nucleotide coenzyme into contact with a sample; a step of detecting a signal corresponding to a change of at least one of the first nucleotide coenzyme and a conversion product thereof, and the second nucleotide coenzyme and a conversion product thereof; and (3) a step of calculating, on the basis of the detected change of the signal, an amount of the kinase forward reaction substrate and/or the phosphorylated product thereof contained in the sample.

Abstract: A measurement method for human pancreatic lipase activity in a sample, includes bringing a bile acid that makes a pH for giving a maximum value of human pancreatic lipase activity to be lower than 7.7, a diglyceride and a colipase into contact with the sample at pH 7.4 or lower; and detecting a signal amount varying in accordance with the human pancreatic lipase activity in the sample, and the bile acid is a bile acid containing: one of or two or more of a-type bile acids selected from the group consisting of GDCA, GCDCA, TDCA, TCDCA and salts thereof; and/or a combination of one of or two or more of b-1-type bile acids selected from the group consisting of GCA, GUDCA, TCA, TUDCA and salts thereof, and one of or two or more of b-2-type bile acids selected from the group consisting of DCA, CDCA and salts thereof.

Abstract: The present invention provides a measuring method for at least one of a kinase forward reaction substrate, a phosphorylated product thereof, and a precursor thereof, and includes a step of conducting an enzymatic cycling reaction by bringing at least a kinase, a first nucleotide coenzyme of the kinase, and a second nucleotide coenzyme having a different nucleoside moiety from the first nucleotide coenzyme into contact with a sample; a step of detecting a signal corresponding to a change of at least one of the first nucleotide coenzyme and a conversion product thereof, and the second nucleotide coenzyme and a conversion product thereof; and (3) a step of calculating, on the basis of the detected change of the signal, an amount of the kinase forward reaction substrate and/or the phosphorylated product thereof contained in the sample.

Abstract: A measurement method for human pancreatic lipase activity in a sample, includes a contact step of bringing a bile acid that makes a pH for giving a maximum value of human pancreatic lipase activity to be lower than 7.7, a diglyceride and a colipase into contact with the sample at pH 7.4 or lower; and a detection step of detecting a signal amount varying in accordance with the human pancreatic lipase activity in the sample, and the bile acid is a bile acid containing: one of or two or more of a-type bile acids selected from the group consisting of GDCA, GCDCA, TDCA, TCDCA and salts thereof; and/or a combination of one of or two or more of b-1-type bile acids selected from the group consisting of GCA, GUDCA, TCA, TUDCA and salts thereof, and one of or two or more of b-2-type bile acids selected from the group consisting of DCA, CDCA and salts thereof.

Abstract: Provided is a novel and useful method of measuring pyrophosphate in a sample. There may be provided a novel and useful method of measuring pyrophosphate in a sample using pyruvate orthophosphate dikinase, nicotinamide-nucleotide adenylyltransferase, and dehydrogenase.

Abstract: Provided is a novel and useful method of measuring pyrophosphate in a sample. There may be provided a novel and useful method of measuring pyrophosphate in a sample using pyruvate orthophosphate dikinase, nicotinamide-nucleotide adenylyltransferase, and dehydrogenase.

Abstract: A method for determining adenosine 5' diphosphate (ADP) contained in a liquid sample by means of an enzymatic reaction, comprising reacting the sample at 15 to 45.degree. C. at least in the presence of glucose, ADP-dependent hexokinase, and oxidized NAD(P), a glucose-6-phosphate dehydrogenase, and one or more salts releasing ions selected among magnesium, cobalt, and manganese ions and then determining the ADP contained in the sample together with the AMP resulting from the reaction based on the amount of the reduced NAD(P) yielded. This method has advantages in that the limit of determination is high because ADP is determined based on the amount of the reduced NAD(P) yielded, and since the reduced NAD(P) has a definite molecular extinction coefficient, the value found is highly reliable and uninfluenced by the reducing substances contained in the sample.