Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1960 Nov;77(2):230–239. doi: 10.1042/bj0770230

Evidence for the chemical interaction of urease in solution

J M Creeth 1,*, L W Nichol 1
PMCID: PMC1204977  PMID: 13696356

Full text

PDF
230

Images in this article

233Fig. 2.
on p.233

Selected References

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

  1. BRIGGS D. R., WOLF W. J. Studies on the cold-insoluble fraction of the water-extractable soybean proteins. I. Polymerization of the 11 S component through reactions of sulfhydryl groups to form disulfide bonds. Arch Biochem Biophys. 1957 Nov;72(1):127–144. doi: 10.1016/0003-9861(57)90180-7. [DOI] [PubMed] [Google Scholar]
  2. CECIL R., McPHEE J. R. A kinetic study of the reactions on some disulphides with sodium sulphite. Biochem J. 1955 Jul;60(3):496–506. doi: 10.1042/bj0600496. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CECIL R., McPHEE J. R. The estimation of thiols and disulphides by potentiometric titration with silver nitrate. Biochem J. 1955 Feb;59(2):234–240. doi: 10.1042/bj0590234. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. EVERT H. E. The reversibility of the mercuric chloride inhibition of urease at varied initial urea concentrations. Arch Biochem Biophys. 1952 Nov;41(1):29–41. doi: 10.1016/0003-9861(52)90501-8. [DOI] [PubMed] [Google Scholar]
  5. HUGGINS C., TAPLEY D. F., JENSEN E. V. Sulphydryl-disulphide relationships in the induction of gels in proteins by urea. Nature. 1951 Apr 14;167(4250):592–593. doi: 10.1038/167592a0. [DOI] [PubMed] [Google Scholar]
  6. Henry R. J., Smith E. C. Use of Sulfuric Acid-Dichromate Mixture in Cleaning Glassware. Science. 1946 Nov 1;104(2705):426–427. doi: 10.1126/science.104.2705.426. [DOI] [PubMed] [Google Scholar]
  7. JOHNSON P., SHOOTER E. M., RIDEAL E. K. The globulins of the ground nut. (Arachis hypogaea) II. Electrophoretic examination of the arachin system. Biochim Biophys Acta. 1950 Jun;5(3/4):376–396. doi: 10.1016/0006-3002(50)90184-3. [DOI] [PubMed] [Google Scholar]
  8. KUFF E. L., HOGEBOOM G. H., STRIEBICH M. J. The sedimentation behavior of alcohol dehydrogenase and urease in crude solutions. J Biol Chem. 1955 Jan;212(1):439–448. [PubMed] [Google Scholar]
  9. O'DONNELL I. J., BALDWIN R. L., WILLIAMS J. W. Correlation of the N=a reaction of thyroglobulin with the type of breakdown produced by papain. Biochim Biophys Acta. 1958 May;28(2):294–308. doi: 10.1016/0006-3002(58)90476-1. [DOI] [PubMed] [Google Scholar]
  10. OGSTON A. G., TILLEY J. M. Studies on the heterogeneity of crystallized beta-lactoglobulin. Biochem J. 1955 Apr;59(4):644–653. doi: 10.1042/bj0590644. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. PEACOCKE A. R., SCHACHMAN H. K. Studies on the sedimentation behaviour of thymus deoxypentose nucleic acid with reference to its homogeneity, size and shape. Biochim Biophys Acta. 1954 Oct;15(2):198–210. doi: 10.1016/0006-3002(54)90060-8. [DOI] [PubMed] [Google Scholar]
  12. SETLOW R. B. The inactivation of urease by deuterons and heat. Arch Biochem Biophys. 1952 Apr;36(2):328–335. doi: 10.1016/0003-9861(52)90418-9. [DOI] [PubMed] [Google Scholar]
  13. WILLS E. D. Enzyme inhibition by suramin and the measurement of the isoelectric points of some enzymes. Biochem J. 1952 Jan;50(3):421–425. doi: 10.1042/bj0500421. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES