A method for determining the sedimentation behavior of enzymes: application to protein mixtures.

  title={A method for determining the sedimentation behavior of enzymes: application to protein mixtures.},
  author={R. Martin and B. Ames},
  journal={The Journal of biological chemistry},
  • R. Martin, B. Ames
  • Published 1961
  • Medicine, Chemistry
  • The Journal of biological chemistry
During an investigation of the gene-enzyme relationships in histidine biosynthesis in Xalmonella typhimurium, it became desirable to determine, in crude extracts, the approximate molecular weights of several enzymes. We have found sucrose gradient centrifugation to be a suitable method for determining sedimentation coefficients of enzymes in protein mixtures. A variety of enzymes of known properties have been studied in the development of the method. Although the separation cell of Yphantis and… Expand
Physical studies on Escherichia coli B RNA polymerase and its subunits.
Abstract The physical properties of the DNA-dependent RNA-polymerase (E.C. of Escherichia coli B have been studied. Sedimentation to equilibrium in the ultracentrifuge resulted in breakdownExpand
The tentative identification in Escherichia coli of a multienzyme complex with glycolytic activity.
The result indicates that Penicillin spheroplasts of Escherichia coli were capable of selectivity compartmenting glycolytic intermediates, and the possible advantages of a gly colytic multienzyme complex are briefly discussed. Expand
[18] Separation of subunits of proteins by zone centrifugation in a density gradient
Publisher Summary The technique of zone centrifugation is used extensively in the purification and analysis of subcellular particles, viruses, nucleic acids, and proteins. The technique promotesExpand
La maltodextrine phosphorylase d'Escherichia coli.
Purification of the polysaccharide phosphorylase which is induced by maltose in Escherichia coli is described. A forty five-fold purification is achieved by heating, two ammonium sulfateExpand
Purification of protoplast-secreted acid phosphatase from baker's yeast. Effect on adenosine triphosphatase activity.
Results suggest that the two activities of acid phosphatase and ATPase are associated with the same protein molecule. Expand
Anthranilate Synthetase, an Enzyme Specified by the Tryptophan Operon of Escherichia coli: Purification and Characterization of Component I
Enzyme activity measurements indicated that wild-type E. coli produces equimolar amounts of at least four of the five polypeptides specified by the operon and purified anthranilate synthetase component I is inhibited by l-tryptophan. Expand
Escherichia coli phosphoenolpyruvate carboxylase: characterization and sedimentation behavior.
  • T. E. Smith
  • Chemistry, Medicine
  • Archives of biochemistry and biophysics
  • 1968
Sedimentation analyses of the enzyme in sucrose gradients indicate association-dissociation reactions involving monomeric units of 94,000 molecular weight, indicating that the dimers of PEP carboxylase are enzymatically active. Expand
Two enzymically active forms of glycyl-tRNA synthetase from Bacillus brevis. Purification and properties.
It is concluded that E1 is a tetrameric protein consisting of two large and two small subunits (alpha2beta2) and E2 is a component of E1 with a structural formula alpha2. Expand
Physical and kinetic properties of lysine-sensitive aspartate kinase purified from carrot cell suspension culture
Abstract Lysine-sensitive aspartate kinase was purified over a 1000-fold from carrot cells grown in suspension culture. A novel staining method was developed to visualise aspartate kinase activity inExpand
A method for the measurement of the sedimentation coefficient and molecular weight of microgram quantities of proteins in 6 M guanidine hydrochloride.
A technique has been perfected for measuring the sedimentation coefficient of microgram quantities of a reduced protein in 6 M guanidine hydrochloride and the results of the application of the method to known proteins are reported. Expand


Some observations on the correlation of genetic information with enzyme molecular weight are discussed
  • J. Gen. Microbiol.,
  • 1960