Acetyl CoA Carboxylase: Isolation and Characterization of Native Biotin Carboxyl Carrier Protein

A large form of biotin carboxyl carrier protein (BCCPL) has been isolated from extracts of Escherichia coli. It has a minimal molecular weight of 20,000, according to its behavior on sodium dodecylsulfate-polyacrylamide gel electrophoresis, and contains approximately 1 mol of biotin per 22,000 g of...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1971-07, Vol.68 (7), p.1512-1515
Main Authors: Fall, R. Ray, Nervi, A. M., Alberts, Alfred W., Vagelos, P. Roy
Format: Article
Language:English
Subjects:
Bacterial Proteins - analysis
Bacterial Proteins - isolation & purification
Biological Sciences: Biochemistry
Biotin - analysis
Carboxylation
Carrier proteins
Coenzyme A
Electrophoresis
Electrophoresis, Disc
Escherichia coli - enzymology
Escherichia coli - growth & development
Gels
Kinetics
Ligases - isolation & purification
Molecular chains
Molecular Weight
Protein Binding
Proteins
Sodium
Sulfates
Tritium
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Description
Summary:A large form of biotin carboxyl carrier protein (BCCPL) has been isolated from extracts of Escherichia coli. It has a minimal molecular weight of 20,000, according to its behavior on sodium dodecylsulfate-polyacrylamide gel electrophoresis, and contains approximately 1 mol of biotin per 22,000 g of protein. BCCPLexhibits Kmvalues, in the biotin carboxylase and transcarboxylase half-reactions of acetyl CoA carboxylase, of 2 × 10-7M and 4 × 10-7M, respectively; these values are 50-100 times lower than those obtained with smaller forms of BCCP previously isolated. Electrophoresis of crude extracts of E. coli indicates that the major biotin-containing protein migrates at the same rate as BCCPL, which suggests that BCCPLis the native form of BCCP in E. coli.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.68.7.1512