Preview this article:
Zoom in

Partial Purification of Glycerate Kinase from sp., Page 1 of 1

| /docserver/preview/fulltext/micro/107/2/mic-107-2-381-1.gif

There is no abstract available for this article.
Use the preview function to the left.


Article metrics loading...

Loading full text...

Full text loading...



  1. Child J., Willetts A. 1978; Microbial metabolism of aliphatic glycols. Bacterial metabolism of ethylene glycol. Biochimica et biophysica acta 538:316–327
    [Google Scholar]
  2. Doughty C. C, Hayashi J. A., Guenther H. L. 1966; Purification and properties of d-glycerate 3-kinase from Escherichia coli . Journal of Biological Chemistry 241:568–572
    [Google Scholar]
  3. Harder W., Attwood M. M., Quayle J. R. 1973; Methanol assimilation by Hyphomicrobium sp. Journal of General Microbiology 78:155–163
    [Google Scholar]
  4. Hill B., Attwood M. M. 1974; The purification of glycerate kinase from Hyphomicrobium sp. and Pseudomonas amI : product identification. Journal of General Microbiology 83:187–190
    [Google Scholar]
  5. Hill B., Attwood M. M. 1976a; Purification and characterization of phosphoglycerate mutase from methanol-grown Hyphomicrobium x and Pseudomonas amI . Journal of General Microbiology 96:185–193
    [Google Scholar]
  6. Hill B., Attwood M. M. 1976b; The effect of adenosine triphosphate on phosphoglycerate mutase activity from Hyphomicrobium x and Pseudomonas amI grown on reduced one-carbon compounds. Journal of General Microbiology 97:335–338
    [Google Scholar]
  7. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  8. Newaz S. S., Hersh L. B. 1975; Reduced nico-tinamide adenine dinucleotide-activated phos-phoenolpyruvate carboxylase in Pseudomonas ma: potential regulation between carbon assimilation and energy production. Journal of Bacteriology 124:825–833
    [Google Scholar]
  9. Roustan C, Brevet A., Pradel L. A., Von Thoai N. 1973; Yeast 3-phosphoglycerate kinase. Interaction of the enzyme with substrates studied by partial isotope exchange and difference spectrophotometry. European Journal of Biochemistry 37:248–255
    [Google Scholar]

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error