A glycine-rich sequence in the catalytic site of F-type ATPase
β Scribed by Masamitsu Futai; Atsuko Iwamoto; Hiroshi Omote; Masatomo Maeda
- Publisher
- Springer US
- Year
- 1992
- Tongue
- English
- Weight
- 438 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0145-479X
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π SIMILAR VOLUMES
Osteopontin (OPN) is a secreted calcium-binding phosphoprotein produced in a variety of normal and pathological contexts, including tissue mineralization and cancer. OPN contains a conserved RGD (arg-gly-asp) amino acid sequence that has been implicated in binding of OPN to cell surface integrins. T
Treatment of P-type ATPases (from mammalian sources) by fluorescein isothiocyanate (ITC) revealed the ITC label on a lysine residue that was than considered as essential for binding of ATP in the ATP-binding site of these enzymes. On the other hand, experiments with site directed mutagenesis exclude