Abstract
An Alteration in the Reactivity of Chymotrypsin and Trypsin towards Hydrogen Peroxide in the Presence of Specific Substrates
Highlights
N-acetylcysteamine (20,000 d.p.m.), 0.25 mg of hydroxylapatitepurified dehydrase, and buffer in a final volume of 1.0 ml
% 20.7-26.5 20.0 26.2 48.3 50.2 lengthening [6], it follows that the E. coli synthetase contains at least two dehydrases
We conclude that this dehydrase accounts for the formation of cisvaccenic acid by the E. coli synthetase and that it is the key enzyme which is responsible for the anaerobic synthesis of unsaturated fatty acids by certain bacterial systems
Summary
Dependence of total dehydration and dehydrase specijicity on phosphate buffer concentration. N-acetylcysteamine (20,000 d.p.m.), 0.25 mg of hydroxylapatitepurified dehydrase, and buffer in a final volume of 1.0 ml. After incubation at 30” for 30 minutes, the thioesters were saponified by the addition of 0.5 ml of 1 N NaOH, followed by incubation at 30” for 10 minutes. After acidification and extraction with ether, the products were separated from 3-C14-3-hydroxydecanoic acid by silicic acid chromatography. Trans-2- and 3-Decenoic acids were separated by gas-liquid chromatography of the methyl esters on a polyethylene glycol succinate column operated at 110” After acidification and extraction with ether, the products were separated from 3-C14-3-hydroxydecanoic acid by silicic acid chromatography. trans-2- and 3-Decenoic acids were separated by gas-liquid chromatography of the methyl esters on a polyethylene glycol succinate column operated at 110”
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
