PURIFICATION AND ACTIVE SITE MODIFICATION OF WHEAT GERM UROGEN I SYNTHASE.

Title: PURIFICATION AND ACTIVE SITE MODIFICATION OF WHEAT GERM UROGEN I SYNTHASE.
Identifier: AAI8023729
identifier: 8023729
Creator: POLLACK, STUART ELKON.
Contributor: Charlotte Russell
Date: 1980
Language: English
Publisher: City University of New York.
Subject: Chemistry, Biochemistry
Abstract: Urogen I synthase was purified from wheat germ. The purification consisted of acid precipitation, ammonium sulfate precipitation, heat denaturation, chromatography by affinity on mercuriphenylagarose followed by DEAE cellulose column chromatography. The molecular weight of the enzyme is 40,000 as judged by calibrated molecular sieve chromatography. The enzyme was inactivated by the arginine specific reagents butanedione and phenylglyoxal and by the lysine specific reagent pyridoxal-5'-phosphate. The stoichiometry of the reaction was 1:1 and the inhibition was lifted by substrate or competitive inhibitor in each case, indicating that the enzyme's active site contains 1 arginine and 1 lysine residue necessary for catalysis.
Type: dissertation
Source: PQT Legacy CUNY.xlsx
degree: Ph.D.
Program: Biochemistry

Media: PURIFICATION AND ACTIVE SITE MODIFICATION OF WHEAT GERM UROGEN I SYNTHASE.