Regioselective Photolabeling of Glycophorin A in Membranes
✍ Scribed by Yoshikatsu Ogawa; Wolfgang Hahn; Philippe Garnier; Nobuaki Higashi; Dominique Massotte; Marie-Hélène Metz-Boutigue; Bernard Rousseau; Masato Kodaka; Junzo Sunamoto; Guy Ourisson; Yoichi Nakatani
- Publisher
- John Wiley and Sons
- Year
- 2002
- Tongue
- English
- Weight
- 143 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0947-6539
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📜 SIMILAR VOLUMES
The topography of membrane-bound proteins at atomic resolution is known only in rare cases. [1] Although the primary amino-acid sequence of glycophorin A (GPA), the major sialoglycoprotein of the human erythrocytes, has been known for more than twenty years and was the first membrane protein sequenc
## Abstract Glycophorin A is the major sialoglycoprotein of the human erythrocyte membrane. Structural studies indicate that this molecule is made up of 3 domains composed of 2 hydrophilic segments which are separated by a region of 22 nonpolar amino acids. The N‐terminal half of the molecule conta
A systematic study of the photoalkylation of amino acids by α-coupling products. Methionine was shown to be favoured both in the sense of reactivity as well as product stability. benzophenone, a standard photosensitive probe of biomolecules, was performed addressing for the first time chemo-, Prelim
## Abstract This report presents an analysis of the phosphorylation of human and rabbit erythrocyte membrane proteins which migrate in NaDodSO~4~‐polyacrylamide gels in the area of the Coomassie Blue‐stained proteins generally known as band 3. The phosphorylation of these proteins is of interest as