Skip to main content
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1989 Dec;55(12):3240–3242. doi: 10.1128/aem.55.12.3240-3242.1989

Simple Method To Detect β-Galactosidase

Tarun Bhowmik 1, Elmer H Marth 1,*
PMCID: PMC203256  PMID: 16348081

Abstract

A simple and rapid method was developed to detect β-galactosidase by using α- or β-naphthyl-β-d-galactopyranoside as substrate and fast garnet GBC as a dye coupler following polyacrylamide gel electrophoresis. This method was specific for β-galactosidase but not for phospho-β-galactosidase.

Full text

PDF
3240

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baldwin K. A., McKay L. L. Spontaneous release of temperate phage by relysogenized lactose-positive transductants of Streptococcus lactis C2. J Dairy Sci. 1987 Oct;70(10):2005–2012. doi: 10.3168/jds.S0022-0302(87)80247-3. [DOI] [PubMed] [Google Scholar]
  2. COHEN R. B., TSOU K-C, RUTENBURG S. H., SELIGMAN A. M. The colorimetric estimation and histochemical demonstration of beta-d-galactosidase. J Biol Chem. 1952 Mar;195(1):239–249. [PubMed] [Google Scholar]
  3. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  4. Jin D. J., Gross C. A. Mapping and sequencing of mutations in the Escherichia coli rpoB gene that lead to rifampicin resistance. J Mol Biol. 1988 Jul 5;202(1):45–58. doi: 10.1016/0022-2836(88)90517-7. [DOI] [PubMed] [Google Scholar]
  5. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  6. MARKERT C. L., HUNTER R. L. The distribution of esterases in mouse tissues. J Histochem Cytochem. 1959 Jan;7(1):42–49. doi: 10.1177/7.1.42. [DOI] [PubMed] [Google Scholar]
  7. McKay L. L., Walter L. A., Sandine W. E., Elliker P. R. Involvement of phosphoenolpyruvate in lactose utilization by group N streptococci. J Bacteriol. 1969 Aug;99(2):603–610. doi: 10.1128/jb.99.2.603-610.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. McKay L., Miller A., 3rd, Sandine W. E., Elliker P. R. Mechanisms of lactose utilization by lactic acid streptococci: enzymatic and genetic analyses. J Bacteriol. 1970 Jun;102(3):804–809. doi: 10.1128/jb.102.3.804-809.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Miller C. G., Mackinnon K. Peptidase mutants of Salmonella typhimurium. J Bacteriol. 1974 Oct;120(1):355–363. doi: 10.1128/jb.120.1.355-363.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Priyolkar M., Nair C. K., Pradhan D. S. Purification and characterisation of an inducible beta-galactosidase from Corynebacterium murisepticum. Arch Microbiol. 1989;151(1):49–53. doi: 10.1007/BF00444668. [DOI] [PubMed] [Google Scholar]
  11. TSOU K. C., SU H. C. A STUDY OF YEAST ALPHA-GALACTOSIDASE WITH NAPHTHYL ALPHA-D-GALACTOPYRANOSIDES AS CHROMOGENIC SUBSTRATES. Anal Biochem. 1964 Aug;8:415–423. doi: 10.1016/0003-2697(64)90239-8. [DOI] [PubMed] [Google Scholar]
  12. WALLENFELS K., MALHOTRA O. P. Galactosidases. Adv Carbohydr Chem. 1961;16:239–298. doi: 10.1016/s0096-5332(08)60264-7. [DOI] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES