Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1969 Dec;64(4):1155–1161. doi: 10.1073/pnas.64.4.1155

STUDY OF CARBONIC ANHYDRASE USING PERTURBED ANGULAR CORRELATIONS OF GAMMA RADIATION*

Claude F Meares 1,2,†, Robert G Bryant 1,2,‡, John D Baldeschwieler 1,2, David A Shirley 1,2
PMCID: PMC223261  PMID: 4989397

Abstract

The angular correlation of the 150-247 kev gamma-ray cascade of 111mCd is strongly perturbed when this nucleus is bound to the enzyme carbonic anhydrase. A comparison of the perturbed angular correlation for the apoenzyme with that for native carbonic anhydrase confirms that the 111mCd binds at the active region of the enzyme. These results provide good evidence that the perturbed angular correlation reflects the effective molecular rotational correlation time at the metal binding site, and that this radioactive nucleus can be used as a rotational tracer to label biological macromolecules. The qualitative dependence of the perturbed angular correlation of the 111mCd cascade on the molecular rotational correlation time at the metal binding site is illustrated using a cadmium-complex solution at various temperatures.

Full text

PDF
1155

Selected References

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

  1. Haugland R. P., Stryer L., Stengle T. R., Baldeschwieler J. D. Nuclear magnetic resonance studies of antibody-hapten interactions using a chloride ion probe. Biochemistry. 1967 Feb;6(2):498–502. doi: 10.1021/bi00854a018. [DOI] [PubMed] [Google Scholar]
  2. LINDSKOG S., MALMSTROM B. G. Metal binding and catalytic activity in bovine carbonic anhydrase. J Biol Chem. 1962 Apr;237:1129–1137. [PubMed] [Google Scholar]
  3. Leipert T. K., Baldeschwieler J. D., Shirley D. A. Applications of gamma ray angular correlations to the study of biological macromolecules in solution. Nature. 1968 Nov 30;220(5170):907–909. doi: 10.1038/220907a0. [DOI] [PubMed] [Google Scholar]
  4. Marshall A. G. Study of a sulfonyl derivative of alpha-chymotrypsin by chlorine nuclear magnetic resonance. Biochemistry. 1968 Jun;7(6):2450–2453. doi: 10.1021/bi00846a054. [DOI] [PubMed] [Google Scholar]
  5. RICKLI E. E., GHAZANFAR S. A., GIBBONS B. H., EDSALL J. T. CARBONIC ANHYDRASES FROM HUMAN ERYTHROCYTES. PREPARATION AND PROPERTIES OF TWO ENZYMES. J Biol Chem. 1964 Apr;239:1065–1078. [PubMed] [Google Scholar]
  6. Stengle T. R., Baldeschwieler J. D. Halide ions as chemical probes for NMR studies of proteins. Proc Natl Acad Sci U S A. 1966 May;55(5):1020–1025. doi: 10.1073/pnas.55.5.1020. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Stryer L., Griffith O. H. A spin-labeled hapten. Proc Natl Acad Sci U S A. 1965 Dec;54(6):1785–1791. doi: 10.1073/pnas.54.6.1785. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Stryer L. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J Mol Biol. 1965 Sep;13(2):482–495. doi: 10.1016/s0022-2836(65)80111-5. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES