MedicGo
The behavior of holo- and apo-forms of bovine superoxide dismutase at low pH.
Metadata
JournalBiochim. Biophys. ActaNot FoundDate
1975-Nov-18
Publication Type
Research Support, U.S. Gov't, P.H.S.
Journal Article
Volume
1975-Nov-18 / 412 : 26-38
Author
Fee JA , Phillips WD
DoiPMIDMESH
Animals
Apoenzymes
Apoproteins
Binding Sites
Cattle
Circular Dichroism
Electron Spin Resonance Spectroscopy
Erythrocytes
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
Protein Binding
Protein Conformation
Spectrophotometry
Spectrophotometry, Ultraviolet
Superoxide Dismutase
Abstract
1. Holo-superoxide dismutase from bovine erythrocytes has been shown to undergo a reversible structural modification in the pH 3-5 range. 2. The spectral alterations observed on changing from neutrality to pH 2 were: a slight attenuation of the 680 nm absorbance; the loss of the 450 nm shoulder, apparent in the optical spectrum of the native protein; and a new band appeared at 330 nm. The circular dichroism at 600 nm was essentially lost while a weak negative band appeared at approx. 380 nm and a positive band at 310 nm. 3. The EPR spectrum was also modified on changing from the native to the low pH form: A parallel increased from approximately 130 to approximately 150 G, g parallel remained unchanged at approximately 2.27, and gm decreased from approximately 2.09 to approximately 2.08. The apparent linewidth remained essentially constant. 4. High resolution (220 MHz) PMR spectra of holo- and apoproteins revealed that the metals influence the three-dimensional structure of the protein. 5. PMR studies indicated that at pH 3 the apoprotein existed almost entirely in a random coil form and that it assumed a compact well-ordered structure on returning to neutral pH. The holoprotein maintained a compact, apparently dimeric, structure even at pH 3.
Fav
Like
Download
Share
Export
Cite
B
Biochim. Biophys. ActaBiochimica et biophysica acta
Metadata
Location
From

No Data

© 2017 - 2020 Medicgo
Powered by some medical students