Synthesis and conformational characterization of the epidermal growth factor-like domain of blood coagulation factor IX carrying xylosyl-glucose
β Scribed by Mayuko Kitamura; Hironobu Hojo; Yoshiaki Nakahara; Takeshi Ishimizu; Sumihiro Hase
- Book ID
- 111583747
- Publisher
- Springer US
- Year
- 2004
- Tongue
- English
- Weight
- 260 KB
- Volume
- 21
- Category
- Article
- ISSN
- 1573-4986
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract The 45βresidue Cβterminal EGFβlike domain in human blood coagulation factor IX has been synthesized by a 2βstep method to form selectively 3 disulfide bridges. Four out of 6 cysteines are blocked with either trityl or 4βmethylβbenzyl, and the remaining 2 cysteines are blocked with aceta
A key step leading to fertilization is the binding of sperm to the egg plasma membrane. When a mammalian sperm reaches the egg plasma membrane, fertilin, an extracellular sperm membrane protein, is believed to bind to an egg plasma membrane receptor mediating fusion. Fertilin is composed of two subu