Abstract
The molecular and functional properties of the ferrous and ferric derivatives of the native and PCMB-reacted main myoglobin component (Mb II) from a marine turtle (Dermochelys coriacea) have been studied. The results are compared with those of other monomeric hemoproteins and have been found to be similar to those of sperm whale myoglobin, considered as a molecular prototype.
Original language | English |
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Pages (from-to) | 281-289 |
Number of pages | 9 |
Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
Volume | 788 |
Issue number | 3 |
DOIs | |
Publication status | Published - Aug 14 1984 |
Keywords
- (D. coriacea)
- Monomeric hemoprotein
- Myoglobin
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
- Structural Biology