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J. Biochem, 1988, Vol. 104, No. 4 606-609
© 1988 Japanese Biochemical Society

research-article

A Comparative Study on the Structural Differences of Primate Hemoglobins by Spin Labeling Technique

Shin-ichi Nakayama*, Mamoru Aoki**, Tokuko Watanabe**,1, Osamu Takenaka***, Kenji Takahashi***,2, Masamatsu Hoshino**** and Masayuki Yoshida*

*University of Library and Information Science Tsukuba, Ibaraki 305
**Department of Chemistry, Faculty of Science, The University of Tokyo Bunkyo.ku, Tokyo 113
***Department of Biochemistry, Primate Research Institute, Kyoto University, Inuyama Aichi 484
****Department of Chemistry, Faculty of Science, Saitama University Urawa, Saitama 338

2Department of Biophysics and Biochemistry, Faculty of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113; to whom correspondence should be addressed

The hemoglobins of human and five non-human primates were spin-labeled with N-(1-oxyl-2,2,6,6-tetramethyl-4-piperidinyl)iodoacetamide, and the ESR spectra of their deoxy, oxy, and carbonmonoxy forms were measured. The analyses of the spectra indicated that the local protein conformation in the vicinity of the spin-labeled cysteine residue at position 93(F9) in the ß-chain is slightly but significantly different among species, and that each hemoglobin shows a similar change in conformation upon conversion from the oxy form to the carbonmonoxy one except for human hemoglobin. Human hemoglobin was suggested to undergo a significantly different conformational change upon this conversion, indicating that it has unique characteristics among the primate hemoglobins.

1Present addresses: Tokyo University of Fisheries, Minato-ku, Tokyo 108.


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