Synthesis and Evaluation of β-Galactosidase-Targeting Spin-Label Probe: 5-O-β-D-Galactosyl-5-hydroxy-1,1,3,3-tetramethylisoindoline-2-oxyl

Heterocycles ◽  
2020 ◽  
Vol 100 (11) ◽  
pp. 1799
Author(s):  
Shingo Sato ◽  
Koya Sugawara ◽  
Hiroyuki Konno ◽  
Tomohiro Ito
Keyword(s):  
Spin Label ◽  
Label Probe

Intracellular viscosity of lymphocytes determined by a 15N spin label probe

1979 ◽  
Vol 36 (2) ◽  
pp. 207-214 ◽  
Author(s):  
W.R Hedrick ◽  
A Mathew ◽  
J.D Zimbrick ◽  
T.W Whaley
Keyword(s):  
Spin Label ◽  
Label Probe

The interaction of ligands with chemically modified phosphorylase b

1976 ◽  
Vol 54 (5) ◽  
pp. 494-499
Author(s):  
D. Brooks ◽  
S. J. W. Busby ◽  
J. R. Griffiths ◽  
G. K. Radda ◽  
O. Avramovic-Zikic
Keyword(s):  
Conformational Changes ◽  
Spin Label ◽  
Native Enzyme ◽  
Carboxyl Groups ◽  
Chemically Modified ◽  
Allosteric Effector ◽  
Spin Resonance ◽  
Label Probe ◽  
Glycine Ethyl Ester ◽  
Modified Enzyme

Phosphorylase b which had been inactivated with 5-diazo-1H-tetrazole was specifically labelled with 4-iodoacetamidosalicylic acid (a fluorescent probe) or with N-(1-oxyl-2,2,6,6,-tetramethyl-4-piperidinyl)iodoacetamide (a spin label probe) so that the binding of ligands and accompanying conformational changes could be determined by fluorescence or electron spin resonance changes, respectively. The allosteric effector, AMP, causes conformational changes similar to those caused in the native enzyme. The affinity of binding of phosphate or AMP to the inhibited protein is the same as for the unmodified protein. The heterotropic interactions between glucose-1-phosphate or glycogen and AMP are much less in the inactivated enzyme than in unmodified phosphorylase. Using a light scattering assay, it is shown that the modified enzyme binds to glycogen less strongly than the native protein.Phosphorylase b which had been inactivated by carbodiimide in the presence of glycine ethyl ester, resulting in the modification of one or more carboxyl groups, was labelled with the spin label probe described above. The modified enzyme has an affinity for AMP similar to that of the native enzyme. AMP binding to the modified enzyme is tightened by glycogen, weakened by glucose-6-phosphate and is unaffected by glucose- 1-phosphate.The actions of 5-diazo-1H-tetrazole and carbodiimide on phosphorylase are discussed in the light of the above observations.

Mapping the location of DATEM in multi-phase systems: Synthesis and characterization of spin-label probe analogues

2019 ◽  
Vol 275 ◽  
pp. 474-479 ◽  
Author(s):  
Sampson Anankanbil ◽  
Jens Henrik Mose ◽  
Bianca Pérez ◽  
Weiwei Cheng ◽  
Jacob Nedergaard Pedersen ◽  
...  
Keyword(s):  
Spin Label ◽  
Synthesis And Characterization ◽  
Label Probe ◽  
Phase Systems ◽  
Multi Phase

Evaluation of glucose-linked nitroxide radicals for use as an in vivo spin-label probe

2014 ◽  
Vol 124 ◽  
pp. 322-327 ◽  
Author(s):  
Shingo Sato ◽  
Masaki Yamaguchi ◽  
Akio Nagai ◽  
Ryo Onuma ◽  
Misaki Saito ◽  
...  
Keyword(s):  
Spin Label ◽  
Nitroxide Radicals ◽  
Label Probe

scholarly journals A spin label probe for the conformational change on conversion of phosphorylasebto phosphorylasea

FEBS Letters ◽  
1972 ◽  
Vol 28 (2) ◽  
pp. 161-164 ◽  
Author(s):  
R.A. Dwek ◽  
J.R. Griffiths ◽  
G.K. Radda ◽  
U. Strauss
Keyword(s):  
Conformational Change ◽  
Spin Label ◽  
Label Probe

scholarly journals Studies on the Interaction of Ligands with Phosphorylase b Using a Spin-Label Probe

1972 ◽  
Vol 30 (2) ◽  
pp. 339-347 ◽  
Author(s):  
Iain D. Campbell ◽  
Raymond A. Dwek ◽  
Nicholas C. Price ◽  
George K. Radda
Keyword(s):  
Spin Label ◽  
Label Probe
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