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Literature DB >> 4924171

Molecular weight of Escherichia coli beta-galactosidase in concentrated solutions of guanidine hydrochloride.

Abstract

The molecular weight of Escherichia coli beta-galactosidase was determined in 6m- and 8m-guanidine hydrochloride by meniscus-depletion sedimentation equilibrium, sedimentation velocity and viscosity. Sedimentation equilibrium revealed heterogeneity with the smallest component having a molecular weight of about 50000. At lower speeds, the apparent weight-average molecular weight is about 80000. By use of a calculation based on an empirical correlation for proteins that are random coils in 6m-guanidine hydrochloride, sedimentation velocity gave a molecular weight of 91000, and the intrinsic viscosity indicated a viscosity-average molecular weight of 84000. Heating in 6m-guanidine hydrochloride lowered the viscosity of beta-galactosidase in a variable manner.

Entities: Chemical Species

Mesh：

Substances：
Guanidines
Galactosidases

Year: 1970 PMID： 4924171 PMCID： PMC1179595 DOI： 10.1042/bj1200255

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

18 in total

1. [Identification, by in vitro complementation and purification, of a peptide fraction of Escherichia coli beta-galactosidase].

Authors: A Ullmann; D Perrin; F Jacob; J Monod
Journal: J Mol Biol Date: 1965-07 Impact factor: 5.469

7. Characterization by in vitro complementation of a peptide corresponding to an operator-proximal segment of the beta-galactosidase structural gene of Escherichia coli.

Authors: A Ullmann; F Jacob; J Monod
Journal: J Mol Biol Date: 1967-03-14 Impact factor: 5.469

Molecular weight of Escherichia coli beta-galactosidase in concentrated solutions of guanidine hydrochloride.

1. [Identification, by in vitro complementation and purification, of a peptide fraction of Escherichia coli beta-galactosidase].

2. Sedimentation equilibrium of paucidisperse systems. Subunit structure of complemented beta-galactosidase.

3. Evidence for pyrrolidone carboxylic acid in beta-galactosidase from E.

4. Effect of nonsense mutations on translation of the lactose operon of Escherichia coli.

5. Effect of limited digestion by proteolytic enzymes on Escherichia coli beta-galactosidase.

6. Re-initiation of polypeptide synthesis and polarity in the lac operon of Escherichia coli.

7. Characterization by in vitro complementation of a peptide corresponding to an operator-proximal segment of the beta-galactosidase structural gene of Escherichia coli.

8. Comparison of beta-galactosidases from normal (i-o+z+) and operator constitutive (i-ocz+) strains of E. coli.

9. Viscosity and density of aqueous solutions of urea and guanidine hydrochloride.

10. The conformational stability of alpha-helical nonpolar polypeptides in solution.

1. Studies on protein multimers. The association-dissociation behaviour of -galactosidase in glycerol.

2. Restoration of beta-galactosidase to Escherichia coli M15. Complementation studies.