Raman spectroscopy of acetylcholine receptor‐rich membranes from <i>Torpedo marmorata</i> and of their isolated components

Aslanian, Dimitrina; Heidmann, Thiérry; Négrerie, Michel; Changeux, Jean‐Pierre

doi:10.1016/0014-5793(83)80324-x

Cited by 25 publications

(18 citation statements)

References 38 publications

(20 reference statements)

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“…About 50 mol phospholipid/mol protein has been found [158]. The presence of this vibration strongly suggests that lipids remain associated with the Ach-receptor purified with this particular detergent.…”

Section: Isolated Ach-receptor Proteinmentioning

confidence: 87%

“…Although a significant fluorescence background was observed in the low frequency range (400-800 cm-I ) very intense and well resolved peaks were recorded between 800-1700 cm-I and 2800-3100 cm-I (Figure la and 2a in [158]). Although a significant fluorescence background was observed in the low frequency range (400-800 cm-I ) very intense and well resolved peaks were recorded between 800-1700 cm-I and 2800-3100 cm-I (Figure la and 2a in [158]).…”

Section: Native Postsynaptic Membranesmentioning

confidence: 95%

“…Fortunately, the 2800-3100 cm -1 region was free of the fluorescence and thus, in our earlier work, only this region has been analysed [158,159]. Raman spectra of these samples were always accompanied by a very high fluorescence background which obscured almost all vibrations in the 400-1800 cm-1 spectral range.…”

Section: Postsynaptic Membranes Without 43 Kda Proteinmentioning

confidence: 96%

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Molecules in Physics, Chemistry, and Biology

Maruani¹

1989

Topics in Molecular Organization and Engineering

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Section: Isolated Ach-receptor Proteinmentioning

confidence: 87%

Section: Native Postsynaptic Membranesmentioning

confidence: 95%

Section: Postsynaptic Membranes Without 43 Kda Proteinmentioning

confidence: 96%

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Molecules in Physics, Chemistry, and Biology

Maruani¹

1989

Topics in Molecular Organization and Engineering

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“…Raman spectroscopy [18,19] is a particularly wellsuited technique to investigate the interaction of proteins because many vibrations are environment-sensitive. However, to analyse the Raman spectra of the receptortoxin complex a method that allows the 2 molecules to be distinguished is required.…”

Section: Introductionmentioning

confidence: 99%

Interaction of modified neurotoxins fromNaja nigricollis with the nicotinic acetylcholine receptor fromTorpedo marmorata A Raman spectroscopy study

et al. 1991

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Two derivatives of or-toxin from Naja nigricollis venom were used in order to study, by resonance Raman spectroscopy, its interaction with tile nicotinic acetylcholine (AcCho) receptor from membranes of Torpedo marmorata electrocytes. The two modified toxins carry either an NO, group bound to Tyr 25 or a nitrophenylthioether (NPS) bound to Trp -'9, The comparison of the spectra of the free and bound derivatized toxins indicates that the environment of Tyr 2s is not perturbed upon binding to the AcCho receptor, but the surroundings of NPS bound to Tfp 29 are changed. This result indicates that Tyr "-s is not involved in binding, while Trp ~ of the ~-toxin may be in contact with the AcCho receptor. Examination of the spectrum of the AcCho receptor membrane after binding of the NPS-Trp toxin discloses some modifications ol ~ the vibrations of the tryptophan and cysteine disulfide bridge of the receptor. These residues are possibly involved in toxin binding.

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“…In an approach to the molecular organisation of membrane fragments rich in acetylcholine receptor (AcChR) purified from Torpedo marmorata electric organ, we made a Raman spectroscopic study of these membranes (Aslanian et al, 1983b). Valuable information was obtained about the conformation of the protein and lipid molecules which compose these subsynaptic membrane fragments.…”

Section: Introductionmentioning

confidence: 99%

A Raman spectroscopic investigation of the lipid state in acetylcholine receptor-rich membranes from Torpedo marmorata.

Aslanian¹,

Négrerie²

1985

The EMBO Journal

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The lipid state in acetylcholine receptor (AcChR)‐rich membranes purified from electric organ of Torpedo marmorata was studied in the temperature interval from 0 degrees C to 35 degrees C using the (C‐H) stretching and (C‐C) skeletal optical vibrations. The Raman spectra of AcChR‐rich membranes, recorded immediately after preparation of the samples, indicate that the lipids are in a predominant triclinic crystalline lattice and do not undergo a phase transition when the temperature increases up to 35 degrees C. However, the polar groups of the lipids appear subject to temperature‐induced variations. After extraction of 43‐kd and other non‐receptor proteins, spectra indicate an order‐disorder phase transition of lipids at approximately 21 degrees C. This transition appears less cooperative than the transition of the membrane lipid extract. The role of the proteins in preservation of the crystalline state of lipids in AcChR‐rich membranes is discussed.

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Raman spectroscopy of acetylcholine receptor‐rich membranes from Torpedo marmorata and of their isolated components

Cited by 25 publications

References 38 publications

Molecules in Physics, Chemistry, and Biology

Molecules in Physics, Chemistry, and Biology

Interaction of modified neurotoxins fromNaja nigricollis with the nicotinic acetylcholine receptor fromTorpedo marmorata A Raman spectroscopy study

A Raman spectroscopic investigation of the lipid state in acetylcholine receptor-rich membranes from Torpedo marmorata.

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