8-(6-Aminohexyl) amino-cyclic ATPR: A new affinity probe for the study of cyclic ADPR-binding proteins

Bioorganic and Medicinal Chemistry Letters

Volumn 7, Issue 13, 1997, Pages 1753-1756

  Zhang, Fang Jie ^a   Sih, Charles J ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

8 (6 AMINOHEXYL)AMINO CYCLIC ADENOSINE TRIPHOSPHATE RIBOSE; ADENOSINE DIPHOSPHATE RIBOSE; BINDING PROTEIN; CALCIUM ION; INOSITOL TRISPHOSPHATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; RYANODINE RECEPTOR; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; BRAIN MICROSOME; CALCIUM CELL LEVEL; CALCIUM MOBILIZATION; CYCLIZATION; ENDOPLASMIC RETICULUM; NONHUMAN; PROTEIN ISOLATION; RAT; SECOND MESSENGER;

EID: 0030810814     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(97)00306-5     Document Type: Article

References (11)

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8. 2O, 300 MHz, pH 2.5) δ 1.40 (m, 4H), 1.67 (m, 4H), 2.98 (t, J = 7.0 Hz, 2H), 3.45 (m, 2H), 4.23-4.38 (m, 3H), 4.46 (m, 1H), 4.59 (m, 1H), 5.95 (brs, 1H), 8.23 (s, 1H).
9. +).
10. +).
11. Preparation of the affinity column: Compound 1 (1.4 mg, 19 μmol) was incubated with pre-swelled cyanogen bromide activated sepharose 4B (3.5 mL) (from Sigma) in 0.1 M sodium bicarbonate (pH 8.3, 20 mL) at 4 °C for 16 h. UV analysis of the solution after filtration revealed that 1.3 mg of 1 was attached onto the resin and HPLC analysis showed that free 1 in the solution remained unchanged. The excess reactive sites on the resin were destroyed by treatment with excess aminoethanol. Incubation of compound 1 in 0.1 M sodium bicarbonate at 4 °C to 23 °C for 24 h did not show significant decomposition from HPLC analysis.