Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1963 Dec;89(3):599–609. doi: 10.1042/bj0890599

Avidin. 3. The nature of the biotin-binding site

N M Green 1,*
PMCID: PMC1202468  PMID: 14101981

Full text

PDF
599

Selected References

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

  1. BIGELOW C. C., GESCHWIND I. I. Difference specta of amino acids and proteins in aqueous media of high refractive index. C R Trav Lab Carlsberg. 1960;31:283–304. [PubMed] [Google Scholar]
  2. BIGELOW C. C., SONENBERG M. The effect of dodecyl sulfate on the ultraviolet spectra of proteins. Biochemistry. 1962 Mar;1:197–204. doi: 10.1021/bi00908a002. [DOI] [PubMed] [Google Scholar]
  3. GLAZER A. N., SMITH E. L. Studies on the ultraviolet difference spectra of proteins and polypeptides. J Biol Chem. 1961 Nov;236:2942–2947. [PubMed] [Google Scholar]
  4. GREEN N. M. AVIDIN. 1. THE USE OF (14-C)BIOTIN FOR KINETIC STUDIES AND FOR ASSAY. Biochem J. 1963 Dec;89:585–591. doi: 10.1042/bj0890585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. GREEN N. M. AVIDIN. 4. STABILITY AT EXTREMES OF PH AND DISSOCIATION INTO SUB-UNITS BY GUANIDINE HYDROCHLORIDE. Biochem J. 1963 Dec;89:609–620. doi: 10.1042/bj0890609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. GREEN N. M. Spectroscopic evidence for the participation of tryptophan residues in the binding of biotin by avidin. Biochim Biophys Acta. 1962 May 7;59:244–246. doi: 10.1016/0006-3002(62)90726-6. [DOI] [PubMed] [Google Scholar]
  7. HERSKOVITS T. T., LASKOWSKI M., Jr Location of chromophoric residues in proteins by solvent perturbation. I. Tyrosyls in serum albumins. J Biol Chem. 1962 Aug;237:2481–2492. [PubMed] [Google Scholar]
  8. KENDREW J. C., WATSON H. C., STRANDBERG B. E., DICKERSON R. E., PHILLIPS D. C., SHORE V. C. The amino-acid sequence x-ray methods, and its correlation with chemical data. Nature. 1961 May 20;190:666–670. doi: 10.1038/190666a0. [DOI] [PubMed] [Google Scholar]
  9. LYNEN F., KNAPPE J., LORCH E., JUETTING G., RINGELMANN E., LACHANCE J. P. [On the biochemical function of biotin. II. Purification and mode of action of beta-methyl-crotonyl-carboxylase]. Biochem Z. 1961;335:123–167. [PubMed] [Google Scholar]
  10. MELAMED M. D., GREEN N. M. AVIDIN. 2. PURIFICATION AND COMPOSITION. Biochem J. 1963 Dec;89:591–599. doi: 10.1042/bj0890591. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. ROSENHECK K., DOTY P. The far ultraviolet absorption spectra of polypeptide and protein solutions and their dependence on conformation. Proc Natl Acad Sci U S A. 1961 Nov 15;47:1775–1785. doi: 10.1073/pnas.47.11.1775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. WATSON H. C., KENDREW J. C. The amino-acid sequence of sperm whale myoglobin. Comparison between the amino-acid sequences of sperm whale myoglobin and of human hemoglobin. Nature. 1961 May 20;190:670–672. doi: 10.1038/190670a0. [DOI] [PubMed] [Google Scholar]
  13. WEBER G. Fluorescence-polarization spectrum and electronic-energy transfer in proteins. Biochem J. 1960 May;75:345–352. doi: 10.1042/bj0750345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. WITKOP B. Nonenzymatic methods for the preferential and selective cleavage and modification of proteins. Adv Protein Chem. 1961;16:221–321. doi: 10.1016/s0065-3233(08)60031-5. [DOI] [PubMed] [Google Scholar]

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

RESOURCES