Details
| Original language | English |
|---|---|
| Pages (from-to) | 533-544 |
| Number of pages | 12 |
| Journal | Journal of applied polymer science |
| Volume | 44 |
| Issue number | 3 |
| Publication status | Published - 25 Jan 1992 |
| Externally published | Yes |
Abstract
Rhodopsin and cyclic guanosine monophosphat (cGMP)‐dependent channel proteins are isolated from the rod outer segment disk membranes of dark‐adopted bovine retinae and incorporated in liposomes, prepared by the method of detergent removal dialysis. The ion channel does not lose its transport function (release of Ca2+ ions by injection of cGMP) when incorporated in a liposome. Its activity depends on the degree of protein solubilization and the kind of detergent used. The highest activity is obtained by use of the detergent CHAPS. Shape, size, and size distribution of the liposomes are deduced from elastic and quasi‐elastic light scattering, the liposome number density by viscometry, and the photopigment or Ca2+ content by optical absorbance. The liposomes are heterogeneous with respect to size and shape. Small unilamellar liposomes (Rh = 80 nm) and a narrow size distribution (UD = 0.16) are obtained by using the detergent CHAPS. With increasing rhodopsin content per liposome, the hydrodynamic radius Rh increases and at the same time the shape of a liposome converts from a sphere to a prolate ellipsoid. The amount of entrapped Ca2+ per liposome reaches its maximum value when the Rhodopsin nearest‐neighbor distance approaches its minimum value. This suggests an intermembrane protein‐lipid‐protein lattice, which serves as barriere for Ca2+. The influence of temperature or total used Ca2+ content is less profound. Increasing temperature yields slightly smaller liposomes.
ASJC Scopus subject areas
- Chemistry(all)
- Materials Science(all)
- Surfaces, Coatings and Films
- Materials Science(all)
- Polymers and Plastics
- Materials Science(all)
- Materials Chemistry
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In: Journal of applied polymer science, Vol. 44, No. 3, 25.01.1992, p. 533-544.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Phospholipid liposomes
T2 - Preparation, characterization, and uses
AU - Nordmeier, E.
AU - Zeilinger, Carsten
AU - Lechner, M. D.
PY - 1992/1/25
Y1 - 1992/1/25
N2 - Rhodopsin and cyclic guanosine monophosphat (cGMP)‐dependent channel proteins are isolated from the rod outer segment disk membranes of dark‐adopted bovine retinae and incorporated in liposomes, prepared by the method of detergent removal dialysis. The ion channel does not lose its transport function (release of Ca2+ ions by injection of cGMP) when incorporated in a liposome. Its activity depends on the degree of protein solubilization and the kind of detergent used. The highest activity is obtained by use of the detergent CHAPS. Shape, size, and size distribution of the liposomes are deduced from elastic and quasi‐elastic light scattering, the liposome number density by viscometry, and the photopigment or Ca2+ content by optical absorbance. The liposomes are heterogeneous with respect to size and shape. Small unilamellar liposomes (Rh = 80 nm) and a narrow size distribution (UD = 0.16) are obtained by using the detergent CHAPS. With increasing rhodopsin content per liposome, the hydrodynamic radius Rh increases and at the same time the shape of a liposome converts from a sphere to a prolate ellipsoid. The amount of entrapped Ca2+ per liposome reaches its maximum value when the Rhodopsin nearest‐neighbor distance approaches its minimum value. This suggests an intermembrane protein‐lipid‐protein lattice, which serves as barriere for Ca2+. The influence of temperature or total used Ca2+ content is less profound. Increasing temperature yields slightly smaller liposomes.
AB - Rhodopsin and cyclic guanosine monophosphat (cGMP)‐dependent channel proteins are isolated from the rod outer segment disk membranes of dark‐adopted bovine retinae and incorporated in liposomes, prepared by the method of detergent removal dialysis. The ion channel does not lose its transport function (release of Ca2+ ions by injection of cGMP) when incorporated in a liposome. Its activity depends on the degree of protein solubilization and the kind of detergent used. The highest activity is obtained by use of the detergent CHAPS. Shape, size, and size distribution of the liposomes are deduced from elastic and quasi‐elastic light scattering, the liposome number density by viscometry, and the photopigment or Ca2+ content by optical absorbance. The liposomes are heterogeneous with respect to size and shape. Small unilamellar liposomes (Rh = 80 nm) and a narrow size distribution (UD = 0.16) are obtained by using the detergent CHAPS. With increasing rhodopsin content per liposome, the hydrodynamic radius Rh increases and at the same time the shape of a liposome converts from a sphere to a prolate ellipsoid. The amount of entrapped Ca2+ per liposome reaches its maximum value when the Rhodopsin nearest‐neighbor distance approaches its minimum value. This suggests an intermembrane protein‐lipid‐protein lattice, which serves as barriere for Ca2+. The influence of temperature or total used Ca2+ content is less profound. Increasing temperature yields slightly smaller liposomes.
UR - http://www.scopus.com/inward/record.url?scp=0026622725&partnerID=8YFLogxK
U2 - 10.1002/app.1992.070440318
DO - 10.1002/app.1992.070440318
M3 - Article
AN - SCOPUS:0026622725
VL - 44
SP - 533
EP - 544
JO - Journal of applied polymer science
JF - Journal of applied polymer science
SN - 0021-8995
IS - 3
ER -