Stability properties of oxymyoglobin from chicken gizzard smooth muscle.
1. Oxymyoglobin (MbO2) was isolated directly from the smooth muscle of chicken gizzard and was examined for its spectral and stability properties. 2. When compared with sperm whale MbO2 as a reference, chicken gizzard MbO2 was found to be much more susceptible to autoxidation. Its pH-dependence was therefore analyzed in terms of an "acid-catalyzed three-state model". 3. The complete amino acid sequence of the myoglobin was also determined. Its hydropathy profile revealed that the region corresponding to the distal side of the heme iron appears to be less hydrophobic.
Biological Institute, Tohoku University, Sendai, Japan.
A
A
Matsuoka
H
H
Iwaasa
K
K
Takiguchi
N
N
Arakawa
L
L
Li
T
T
Takagi
K
K
Shikama
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D005895:Gizzard, Avian; D007700:Kinetics; D008969:Molecular Sequence Data; D009130:Muscle, Smooth / Q000378:metabolism*; D009211:Myoglobin / Q000302:isolation & purification / Q000378:metabolism*; D010084:Oxidation-Reduction
D009211:Myoglobin; C017595:oxymyoglobin