This site needs JavaScript to work properly. Please enable it to take advantage of the complete set of features!

Skip to main page content

Add to Collections

Your saved search

Name of saved search:

Search terms:

Test search terms

Would you like email updates of new search results?

Yes
No

Email: (change)

Frequency:

Which day?

Which day?

Report format:

Send at most:

Send even when there aren't any new results

Optional text in email:

Your RSS Feed

. 1968 Nov 23;220(5169):787-8.

doi: 10.1038/220787a0.

Spin-labelled haemoglobin and the haem-haem interaction

H M McConnell, S Ogawa, A Horwitz

PMID: 4302193
DOI: 10.1038/220787a0

Spin-labelled haemoglobin and the haem-haem interaction

H M McConnell et al. Nature. 1968.

. 1968 Nov 23;220(5169):787-8.

doi: 10.1038/220787a0.

Authors

H M McConnell, S Ogawa, A Horwitz

PMID: 4302193
DOI: 10.1038/220787a0

No abstract available

PubMed Disclaimer

Similar articles

ELECTRON SPIN RESONANCE IN HAEMIN, HAEMATIN AND HAEMOGLOBIN AT 4.2 DEGREES K.
SCHOFFA G. SCHOFFA G. Nature. 1964 Aug 8;203:640-1. doi: 10.1038/203640a0. Nature. 1964. PMID: 14250976 No abstract available.
Changes in EPR spectra of M-type abnormal haemoglobins induced by deoxygenation and their implications for the haem-haem interaction.
Hayashi A, Suzuki T, Shimizu A, Morimoto H, Watari H. Hayashi A, et al. Biochim Biophys Acta. 1967 Oct 23;147(2):407-9. doi: 10.1016/0005-2795(67)90426-6. Biochim Biophys Acta. 1967. PMID: 4294493 No abstract available.
Haem localization in haemoproteins by spin and triplet tools.
Yudanova Y, Meckler V, Fogel V, Kulikov A, Kotelnikov A, Likhtenstein G, Berkovich M, Karyakin A, Archakov A, Kaplun A, et al. Yudanova Y, et al. Eur J Biochem. 1986 May 2;156(3):541-4. doi: 10.1111/j.1432-1033.1986.tb09613.x. Eur J Biochem. 1986. PMID: 2422031
Mössbauer spectroscopy of haem proteins.
Lang G. Lang G. Q Rev Biophys. 1970 Feb;3(1):1-60. doi: 10.1017/s0033583500004406. Q Rev Biophys. 1970. PMID: 4314326 Review. No abstract available.
Spin-label studies of cooperative oxygen binding to hemoglobin.
McConnell HM. McConnell HM. Annu Rev Biochem. 1971;40:227-36. doi: 10.1146/annurev.bi.40.070171.001303. Annu Rev Biochem. 1971. PMID: 4330577 Review. No abstract available.

See all similar articles

Cited by

Nuclear magnetic resonance study of heme-heme interaction in hemoglobin M Milwaukee: implications concerning the mechanism of cooperative ligand binding in normal hemoglobin.
Fung LW, Minton AP, Ho C. Fung LW, et al. Proc Natl Acad Sci U S A. 1976 May;73(5):1581-5. doi: 10.1073/pnas.73.5.1581. Proc Natl Acad Sci U S A. 1976. PMID: 1064027 Free PMC article.
Biophysics with nitroxyl radicals.
Axel FS. Axel FS. Biophys Struct Mech. 1976 Dec 22;2(3):181-218. doi: 10.1007/BF00535367. Biophys Struct Mech. 1976. PMID: 189853
Electron paramagnetic resonance studies of spin-labeled hemoglobins and their implications to the nature of cooperative oxygen binding to hemoglobin.
Ho C, Baldassare JJ, Charache S. Ho C, et al. Proc Natl Acad Sci U S A. 1970 Jul;66(3):722-9. doi: 10.1073/pnas.66.3.722. Proc Natl Acad Sci U S A. 1970. PMID: 4316679 Free PMC article.

MeSH terms

Actions
Actions
Actions
Actions
Actions

Substances

Actions
Actions

LinkOut - more resources

Full Text Sources
- Nature Publishing Group
Other Literature Sources
- The Lens - Patent Citations Database