ライフサイエンスコーパス: erythrosin

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1 of the active enzyme, we labeled SERCA with erythrosin 5'-iodoacetamide, which binds to the phosphor

2 Previous TPA studies on SERCA used primarily erythrosin 5'-isothiocyanate (ErITC), which binds to the

3 rized phosphorescence from the triplet probe erythrosin-5-iodoacetamide attached to sulfhydryls in ra

4 nce emission anisotropy of the triplet probe erythrosin-5-iodoacetamide covalently attached to cystei

5 ission anisotropy (rFA) of the triplet probe erythrosin-5-iodoacetamide covalently bound to Cys-374 o

6 hich FITC labeled the high affinity site and erythrosin-5-isothiocyanate (ErITC) labeled the low affi

7 determinations made between LY as donor and erythrosin-5-isothiocyanate, covalently bound at the enz

8 horescence emission energy and lifetime from erythrosin B dispersed in the matrices indicated that su

9 study illustrates that phosphorescence from erythrosin B is sensitive both to local dipolar relaxati

10 constants for the inhibition by vanadate and erythrosin B remain unchanged.

11 y-state and time-resolved phosphorescence of erythrosin B to monitor mobility in thin films of amorph

12 known Abeta monomer aggregation modulators, Erythrosin B, Eosin Y, Phloxine B, and Rose Bengal, were

13 Calyculin A and erythrosin B, intracellular inhibitors of phosphatases a

14 resolved phosphorescence anisotropy (TPA) of erythrosin iodoacetamide (ErIA) attached to Cys 374 on a

15 ard RLC labeled specifically at Cys 108 with erythrosin iodoacetamide (ErIA).

16 th erythrosin isothiocyanate (ERITC) or with erythrosin iodoacetamide (ERIA).

17 nce (TPA) and absorption anisotropy (TAA) of erythrosin iodoacetamide attached to Cys374 on actin.

18 phosphorescence lifetime of the actin-bound erythrosin iodoacetamide: while muscle S1 increases the

19 etect the microsecond rotational dynamics of erythrosin-iodoacetamide-labeled actin strongly bound to

20 nitor the microsecond rotational dynamics of erythrosin-iodoacetamide-labeled actin with strongly bou

21 cs of actin filaments labeled at Cys374 with erythrosin-iodoacetemide (ErIA), using time-resolved pho

22 sarcoplasmic reticulum (SR) membranes using erythrosin isothiocyanate (Er-ITC) have been identified.

23 ly bound the long-lived phosphorescent probe erythrosin isothiocyanate (Er-ITC) to cytoplasmic sequen

24 rmit the specific and covalent attachment of erythrosin isothiocyanate (Er-ITC) to Lys464 within the

25 which Ca-ATPase was covalently labeled with erythrosin isothiocyanate (ERITC) or with erythrosin iod

26 urements using phosphorescence anisotropy of erythrosin isothiocyanate at Lys464 on the Ca-ATPase pro

27 oscopy to measure the rotational dynamics of erythrosin isothiocyanate covalently bound to Lys464 in

28 rescence anisotropy decay measurements using erythrosin-labeled M5.

29 An erythrosin solution was used for the ultrasonic scaler c

30 The number of squares containing a red erythrosin spot were counted and considered to represent

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