Abstract: A thermoelectric power generation system includes a shell-and-tube heat exchanger configured such that a tube including double tubes of an inner tube and an outer tube is inserted into a shell, and a thermoelectric power generation module inserted into between the inner tube and the outer tube. The thermoelectric power generation module generates thermoelectric power using a temperature difference between a first medium flowing in the inner tube, such as coolant, and a second medium flowing outside the outer tube in the shell, such as excess water vapor.

Abstract: A thermoelectric power generation system 20 includes a heat exchanger 1 having double tubes which are an inner tube 1a and an outer tube 1b, and a thermoelectric power generation module 2 mounted between the inner tube and the outer tube. The thermoelectric power generation module generates thermoelectric power using a temperature difference between a medium inside the inner tube and a medium outside the outer tube, and a highly thermal conductive elastic sheet 3a, 3b is mounted between the thermoelectric power generation module and the inner tube and/or the outer tube in close contact therewith.

Abstract: A reagent for amylase isozyme activity assay, which contains 2-chloro-4-nitrophenyl 4-O-&bgr;-D-galactopyranosylmaltoside, an antibody inhibiting S-type amylase activity or P-type amylase activity, and an amylase activator, and methods for assaying amylase isozyme activity using the regent is provided. According to the present invention, amylase isozyme activity can be accurately and easily assayed using a low concentration activator and an antibody having S-type amylase or P-type amylase activity inhibitory action without using an adjuvant enzyme.

Abstract: A reagent for determining a-amylase activity, comprising a maltooligosaccharide derivative of the following formula ##STR1## (wherein either one of R.sub.1 and R.sub.2 is .beta.-galactopyranosil and the other is hydrogen, R.sub.3 is a group bonded to the reducing terminal glucose via a bond cleavable by .alpha.-amylase, which becomes a measurable substance upon cleavage of the bond, and n is an integer of 0-2), which does not comprise adjuvant enzymes; and a method for determining .alpha.-amylase activity which comprises use of the reagent. The reagent of the present invention does not require use of any adjuvant enzyme and is stable since the substrate is not exposed to the decomposition by an adjuvant enzyme. The substrate used in the present invention has high affinity for .alpha.-amylase. Thus, the reagent and the determination method of the present invention make it possible to determine .alpha.-amylase activity with high sensitivity.