✦ LIBER ✦

Direct observation of binding between biotinylated okadaic acids and protein phosphatase 2A monitored by surface plasmon resonance

✍ Scribed by Keiichi Konoki; Naoyuki Sugiyama; Michio Murata; Kazuo Tachibana

Book ID: 104260480
Publisher: Elsevier Science
Year: 1999
Tongue: French
Weight: 244 KB
Volume: 40
Category: Article
ISSN: 0040-4039
DOI: 10.1016/s0040-4039(98)02474-5

No coin nor oath required. For personal study only.

✦ Synopsis

Two biotin conjugates ofokadaic acid were synthesized for evaluating their interactions with protein phosphatase 2A by surface plasmon resonance (SPR). C7-biotinylated okadaic acid revealed strong binding affinity to the enzyme, while Cl-biotinylated derivative being devoid of affinity, implying that the C7-biotin conjugate is a useful tool for biochemical studies of protein phosphatase 2A.

📜 SIMILAR VOLUMES

Characterization of the Protein Phosphat

Characterization of the Protein Phosphatase 1-Binding Motifs of Inhibitor-2 and DARPP-32 by Surface Plasmon Resonance

✍ Lin, T.-H. 📂 Article 📅 2005 🏛 Oxford University Press 🌐 English ⚖ 195 KB

Correlation between Direct Binding Abili

Correlation between Direct Binding Ability of SyntheticT. gondiiSAG1 Peptides to HLA-A2 Measured by a Sensor for Surface Plasmon Resonance and Antigenicity of the Peptides forT. gondii-Infected Cell-Specific CTL

✍ Akihiko Yano; Fumie Aosai; Tian-Hui Yang; Na He; Hye-Seong Mun; Hui Liu; Hidetos 📂 Article 📅 1997 🏛 Elsevier Science 🌐 English ⚖ 106 KB