Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1959 Dec;78(6):792–795. doi: 10.1128/jb.78.6.792-795.1959

LOCALIZATION AND CHARACTERIZATION OF AN UNUSUALLY HEAT RESISTANT INORGANIC PYROPHOSPHATASE FROM AZOTOBACTER AGILIS1

Emmett J Johnson a, Mary K Johnson b
PMCID: PMC290634  PMID: 14407439

Full text

PDF
792

Selected References

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

  1. ALEXANDER M. Localization of enzymes in the microbial cell. Bacteriol Rev. 1956 Jun;20(2):67–93. doi: 10.1128/br.20.2.67-93.1956. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Alexander M., Wilson P. W. ENZYME LOCALIZATION IN Azotobacter Vinelandii. Proc Natl Acad Sci U S A. 1955 Nov 15;41(11):843–848. doi: 10.1073/pnas.41.11.843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. COTA-ROBLES E. H., MARR A. G., NILSON E. H. Submicroscopic particles in extracts of Azotobacter agilis. J Bacteriol. 1958 Mar;75(3):243–252. doi: 10.1128/jb.75.3.243-252.1958. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. DARTER R. W., MILLMAN I. Localization of mycobacterial enzymes. Proc Soc Exp Biol Med. 1957 Jul;95(3):440–446. doi: 10.3181/00379727-95-23245. [DOI] [PubMed] [Google Scholar]
  5. KORNBERG A. Pyrophosphorylases and phosphorylases in biosynthetic reactions. Adv Enzymol Relat Subj Biochem. 1957;18:191–240. doi: 10.1002/9780470122631.ch5. [DOI] [PubMed] [Google Scholar]
  6. LAWRENCE N. L., HALVORSON H. O. Studies on the spores of aerobic bacteria. IV. A heat resistant catalase from spores of Bacillus terminalis. J Bacteriol. 1954 Sep;68(3):334–337. doi: 10.1128/jb.68.3.334-337.1954. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. LEVINSON H. S., SLOAN J. D., Jr, HYATT M. T. Pyrophosphatase activity of Bacillus megaterium spore and vegetative cell extracts. J Bacteriol. 1958 Mar;75(3):291–299. doi: 10.1128/jb.75.3.291-299.1958. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. MARR A. G., COTA-ROBLES E. H. Sonic disruption of Azotobacter vinelandil. J Bacteriol. 1957 Jul;74(1):79–86. doi: 10.1128/jb.74.1.79-86.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. MARSH C., MILITZER W. Thermal enzymes. V. Properties of a malic dehydrogenase. Arch Biochem Biophys. 1952 Apr;36(2):269–275. doi: 10.1016/0003-9861(52)90411-6. [DOI] [PubMed] [Google Scholar]
  11. MARSH C., MILITZER W. Thermal enzymes. VII. Further data on an adenosinetriphosphatase. Arch Biochem Biophys. 1956 Feb;60(2):433–438. doi: 10.1016/0003-9861(56)90448-9. [DOI] [PubMed] [Google Scholar]
  12. MARSH C., MILITZER W. Thermal enzymes. VIII. Properties of a heat-stable inorganic pyrophosphatase. Arch Biochem Biophys. 1956 Feb;60(2):439–451. doi: 10.1016/0003-9861(56)90449-0. [DOI] [PubMed] [Google Scholar]
  13. MILITZER W., BURNS L. Thermal enzymes. VI. Heat stability of pyruvic oxidase. Arch Biochem Biophys. 1954 Sep;52(1):66–73. doi: 10.1016/0003-9861(54)90089-2. [DOI] [PubMed] [Google Scholar]
  14. MILITZER W., SONDEREGGER T. B., TUTTLE L. C. Thermal enzymes. II. Cytochromes. Arch Biochem. 1950 Apr;26(2):299–306. [PubMed] [Google Scholar]
  15. MILITZER W., TUTTLE L. C., GEORGI C. E. Thermal enzymes. III. Apyrase from a thermophilic Bacterium. Arch Biochem Biophys. 1951 May;31(3):416–423. doi: 10.1016/0003-9861(51)90157-9. [DOI] [PubMed] [Google Scholar]
  16. MILITZER W., TUTTLE L. C. Thermal enzymes. IV. Partial separation of an adenosinetriphosphatase from an apyrase fraction. Arch Biochem Biophys. 1952 Aug;39(2):379–386. doi: 10.1016/0003-9861(52)90347-0. [DOI] [PubMed] [Google Scholar]
  17. STORCK R., WACHSMAN J. T. Enzyme localization in Bacillus megaterium. J Bacteriol. 1957 Jun;73(6):784–790. doi: 10.1128/jb.73.6.784-790.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. THOMPSON T. L., MILITZER W. E., GEORGI C. E. Partial denaturation of a bacterial aldolase without loss of activity. J Bacteriol. 1958 Oct;76(4):337–341. doi: 10.1128/jb.76.4.337-341.1958. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES