A comparative study on the structural differences of primate hemoglobins by spin labeling technique.
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 beta-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.
Nakayama
S
S
University of Library and Information Science, Ibaraki.
Aoki
M
M
Watanabe
T
T
Takenaka
O
O
Takahashi
K
K
Hoshino
M
M
Yoshida
M
M
D000818:Animals; D002263:Carboxyhemoglobin / Q000032:analysis; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D006454:Hemoglobins / Q000032:analysis*; D006801:Humans; D010108:Oxyhemoglobins / Q000032:analysis; D011323:Primates / Q000097:blood*; D011487:Protein Conformation
D006454:Hemoglobins; D010108:Oxyhemoglobins; C100003:deoxyhemoglobin; D002263:Carboxyhemoglobin