Mass spectrometric analysis of rabbit and bovine trypsin-solubilized cytochrome b5
โ Scribed by Bradford W. Gibson; Arnold M. Falick; James J. Lipka; Lucy A. Waskell
- Book ID
- 112460893
- Publisher
- Springer
- Year
- 1990
- Tongue
- English
- Weight
- 850 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1573-4943
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
The crystal structure of the recombinant trypsin-solubilized fragment of the microsomal cytochrome b 5 from bovine liver has been determined at 1.9 ร resolution and compared with the reported crystal structure of the lipase-solubilized fragment of the membrane protein cytochrome b 5 . The two struct
## Abstract Nanoโelectrosprayโionization mass spectrometry (nanoโESIโMS) is applied to comparison of bovine and porcine ฮฒโlactoglobulin (BLG and PLG). The conformational and oligomeric properties of the two proteins under different solvent and experimental conditions are analyzed. The pHโdependence
## Abstract Cytochrome __c__ is a key mitochondrial respiratory protein that is particularly susceptible to modification during oxidative stress. The nature of this susceptibility is linked to the mitochondrial membrane being rich in esterified linoleic acid, which predisposes this organelle to the