COUPLED REACTIONS IN METAMORPHISM: A CORRECTION

Author(s):  
W. S. FYFE ◽  
F. J. TURNER ◽  
J. VERHOOGEN
Keyword(s):  
Author(s):  
Dennis Sherwood ◽  
Paul Dalby

Another key chapter, examining reactions in solution. Starting with the definition of an ideal solution, and then introducing Raoult’s law and Henry’s law, this chapter then draws on the results of Chapter 14 (gas phase equilibria) to derive the corresponding results for equilibria in an ideal solution. A unique feature of this chapter is the analysis of coupled reactions, once again using first principles to show how the coupling of an endergonic reaction to a suitable exergonic reaction results in an equilibrium mixture in which the products of the endergonic reaction are present in much higher quantity. This demonstrates how coupled reactions can cause entropy-reducing events to take place without breaking the Second Law, so setting the scene for the future chapters on applications of thermodynamics to the life sciences, especially chapter 24 on bioenergetics.


2017 ◽  
Vol 258 ◽  
pp. 727-734 ◽  
Author(s):  
Franco Martín Zanotto ◽  
Ricardo Ariel Fernández ◽  
Sergio Alberto Dassie

2018 ◽  
pp. 171-174
Author(s):  
Edward K. Yeargers
Keyword(s):  

1997 ◽  
Vol 119 (35) ◽  
pp. 8332-8341 ◽  
Author(s):  
Michael Meot-Ner (Mautne ◽  
Yezdi B. Pithawalla ◽  
Junling Gao ◽  
M. Samy El-Shall

1991 ◽  
Vol 37 (8) ◽  
pp. 1323-1328
Author(s):  
Z Ogawa ◽  
Y Matsubayashi ◽  
S Satoh ◽  
N Orita ◽  
H Itoh

Abstract We synthesized o-(4,6-o-isopropylidene-alpha-D-glucopyranosyl)-(1----4)- [o-alpha-D-glucopyranosyl-(1----4])5-o-alpha-D-glucopyranosyl-(1----2)- alpha-D-fructofuranoside (IPG7F) and developed an assay for determining the activity of amylase in human serum and urine by using this substrate. Glucoamylase, alpha-glucosidase, and mannitol dehydrogenase are used as coupling enzymes. The coupled reactions are monitored by continuously measuring the oxidation rate of NADH. In this procedure, various substances in the test specimens do not interfere with the detection of amylase activity. Exactly one molecule of NADH is oxidized by one attack of amylase on the substrate, although four products can be produced in the reaction. The within-assay coefficient of variation (CV) ranged from 1.0% to 4.1% and the between-assay CV ranged from 2.6% to 5.3%. The results of our new assay correlate well with those of the amylase assay involving p-nitrophenol maltoheptaoside as substrate (r = 0.978) and with those of the amylase assay involving maltopentaose (r = 0.987).


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