Purification and Properties of Phosphotransacetylase from Veillonella alcalescens

Gel filtration of phosphotransacetylase purified from Veillonella alcalescens gave a molecular weight of 75,000 to 80,000. Ultracentrifugation and sedimentation in sucrose gradients showed a heterogeneous distribution of proteins. The predominant component in sucrose gradients had a sedimentation co...

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Veröffentlicht in:	The Journal of biological chemistry 1972-03, Vol.247 (6), p.1911-1917
Hauptverfasser:	Whiteley, H R, Pelroy, R A
Format:	Artikel
Sprache:	eng
Schlagworte:	Acyltransferases - isolation & purification Ammonium Sulfate Centrifugation, Density Gradient Chromatography, DEAE-Cellulose Chromatography, Gel Coenzyme A Dicarboxylic Acids Drug Stability Electrophoresis Imides Mercaptoethanol Molecular Weight Peptides Protein Denaturation Sodium Dodecyl Sulfate Species Specificity Ultracentrifugation Urea Veillonella - enzymology
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Zusammenfassung:	Gel filtration of phosphotransacetylase purified from Veillonella alcalescens gave a molecular weight of 75,000 to 80,000. Ultracentrifugation and sedimentation in sucrose gradients showed a heterogeneous distribution of proteins. The predominant component in sucrose gradients had a sedimentation coefficient of 4.2; a minor component having a sedimentation coefficient of 2.8 could also be detected. Denaturation with urea or sodium dodecyl sulfate yielded a single polypeptide with a molecular weight of 32,000 to 40,000. Amidination with dimethyl suberimidate prior to denaturation indicated that the enzyme contained two subunits. The properties of this phosphotransacetylase were compared with those of phosphotransacetylases isolated from other bacteria.
ISSN:	0021-9258 1083-351X
DOI:	10.1016/S0021-9258(19)45557-9