Spin-label study of immiscible polymers: 3. Location of chain ends in a blend of polystyrene and polyisoprene

Polymer ◽  
1993 ◽  
Vol 34 (1) ◽  
pp. 25-28 ◽  
Author(s):  
G.G. Cameron ◽  
M.Y. Qureshi ◽  
E. Ross ◽  
I.S. Miles ◽  
J. Richardson
Keyword(s):  
Spin Label ◽  
Label Study ◽  
Immiscible Polymers

Blends of immiscible polymers compatibilized with block copolymer: A spin-label study

1996 ◽  
Vol 32 (5) ◽  
pp. 587-591 ◽  
Author(s):  
G.G. Cameron ◽  
M.Y. Qureshi ◽  
S.C. Tavern
Keyword(s):  
Block Copolymer ◽  
Spin Label ◽  
Label Study ◽  
Immiscible Polymers

Spin-label study of immiscible polymers—II. Influence of polyisoprene on end-labelled polystyrene

1991 ◽  
Vol 27 (11) ◽  
pp. 1181-1186 ◽  
Author(s):  
G.G. Cameron ◽  
M.Y. Qureshi ◽  
E. Ross ◽  
I.S. Miles ◽  
J. Richardson
Keyword(s):  
Spin Label ◽  
Label Study ◽  
Immiscible Polymers

Spin-label study of immiscible polymers—1. Interfacial tension between polystyrene and polyisoprene

1991 ◽  
Vol 27 (8) ◽  
pp. 773-774 ◽  
Author(s):  
G.G. Cameron ◽  
E. Ross ◽  
I.S. Miles ◽  
J. Richardson ◽  
D. Bye
Keyword(s):  
Interfacial Tension ◽  
Spin Label ◽  
Label Study ◽  
Immiscible Polymers

scholarly journals A spin label study of the thyroid hormone-binding sites in human plasma thyroxine transport proteins.

1981 ◽  
Vol 256 (2) ◽  
pp. 831-836
Author(s):  
S.Y. Cheng ◽  
G. Rakhit ◽  
F. Erard ◽  
J. Robbins ◽  
C.F. Chignell
Keyword(s):  
Thyroid Hormone ◽  
Human Plasma ◽  
Spin Label ◽  
Binding Sites ◽  
Transport Proteins ◽  
Hormone Binding ◽  
Label Study

scholarly journals Spin-label study of hemoglobin conformations in solution.

1967 ◽  
Vol 58 (1) ◽  
pp. 19-26 ◽  
Author(s):  
S. Ogawa ◽  
H. M. McConnell
Keyword(s):  
Spin Label ◽  
Label Study

The Orientation of Cytochrome c Oxidase in Coupled Phospholipid Membrane Vesicles—A Spin-Label Study

1975 ◽  
Vol 53 (3) ◽  
pp. 364-370 ◽  
Author(s):  
J. A. Kornblatt ◽  
W. L. Chen ◽  
J. C. Hsia ◽  
G. R. Williams
Keyword(s):  
Molecular Weight ◽  
Binding Site ◽  
Cytochrome Oxidase ◽  
Spin Label ◽  
Resonance Spectrum ◽  
Membrane Vesicles ◽  
Phospholipid Membrane ◽  
Vesicle Membrane ◽  
Exterior Surface ◽  
Label Study

Cytochrome oxidase, an enzyme containing six different subunits, has been shown to span the inner mitochrondrial membrane. The arrangement of the subunits within the membrane is unknown. We have specifically labeled the 25 000 molecular weight subunit with a spin-label derivative of N-ethylmaleimide, 3-maleimido-2,2,5,5-tetramethyl-1-pyrrolidinyloxyl (NEM-SL(5)). NEM-SL(5)-labeled cytochrome oxidase can be incorporated into phospholipid membranes to form coupled vesicles of the Hinkle, Kim &Racker ((1972) J. Biol. Chem. 247, 1338–1339) type. The resonance spectrum of NEM-SL(5) is similar in both soluble and vesicular cytochrome oxidase. Since ascorbate has been shown to reduce only spin label that is exposed to the exterior surface of a closed vesicle, we have used ascorbate to determine the NEM-SL(5)-binding site in the coupled vesicles. NEM-SL(5)-labeled cytochrome oxidase vesicles are reduced by 10 mM ascorbate with [Formula: see text] of 1 min at 22 °C. The rate of reduction is relatively independent of temperature. We conclude that (1) cytochrome oxidase is unidirectionally or preferentially oriented in the vesicle membrane, and (2) the NEM-SL(5)-binding site on the 25 000 molecular weight subunit is exposed to the external aqueous medium.

scholarly journals Changes of Membrane Fluidity in Erythrocytes of Obese Children: A Spin Label Study

1987 ◽  
Vol 22 (2) ◽  
pp. 141-144 ◽  
Author(s):  
Giovanna Curatola ◽  
Gianna Ferretti ◽  
Enrico Bertoli ◽  
Maria Dotti ◽  
Edoardo Bartolotta ◽  
...  
Keyword(s):  
Membrane Fluidity ◽  
Spin Label ◽  
Obese Children ◽  
Label Study
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