Purification and Properties of Rat Liver Microsomal Esterases

Several rat liver microsomal esterases have been isolated. One of these was purified to homogeneity and its physical and catalytic properties were investigated. The enzyme is composed of two subunits of equal molecular weight. Each 70,000 molecular weight subunit appears to have an active site. Evid...

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Veröffentlicht in:	The Journal of biological chemistry 1974-05, Vol.249 (9), p.2717-2722
Hauptverfasser:	Haugen, David A., Suttie, John W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetone Animals Binding Sites Butyrates - metabolism Carboxylic Acids Catalysis Chromatography Chromatography, Gel Chromatography, Ion Exchange Electrophoresis, Disc Esterases - analysis Esterases - antagonists & inhibitors Esterases - isolation & purification Fatty Acids - metabolism Hydrogen-Ion Concentration Liver - cytology Macromolecular Substances Male Microsomes, Liver - enzymology Molecular Weight Rats Sodium Dodecyl Sulfate Structure-Activity Relationship Surface-Active Agents
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Beschreibung
Zusammenfassung:	Several rat liver microsomal esterases have been isolated. One of these was purified to homogeneity and its physical and catalytic properties were investigated. The enzyme is composed of two subunits of equal molecular weight. Each 70,000 molecular weight subunit appears to have an active site. Evidence is presented which suggests that catalysis involves the formation of an acyl-enzyme intermediate and requires the presence of an unprotonated residue with a pK of about 6.0.
ISSN:	0021-9258 1083-351X
DOI:	10.1016/S0021-9258(19)42688-4