In Situ Modification of the Phospholipid Environment of Native Rabbit Sarcoplasmic Reticulum Membranes

B. Szalontai, L. Vígh, F. Joo, L. Senak, R. Mendelsohn

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

A water soluble hydrogenation catalyst (palladium di(sodium alizarine monosulphonate)) in a deuterium-containing environment has been used for the in situ insertion of deuterium atoms into the fatty acyl chains of biological membranes. The thermotropic response of the stretching vibrations of the formed C-D bonds, as detected by Fourier transform IR spectroscopy, was used as a selective probe of biological membrane structure. Partial deuteration of unsaturated fatty acyl chains coupled with IR detection potentially provides a means for detecting specific biological roles of particular lipid classes. In the current study of sarcoplasmic reticulum membranes and purified phospholipid/CaATPase vesicles, it is also shown that νC-D monitors change at particular membrane locations which may remain undetected through the CH2 symmetric stretching frequency, a widely used IR spectral parameter. The latter reflects the average environment of the acyl chains. The approach described here may be suitable for wide applications to the study of biomembranes.

Original languageEnglish
Pages (from-to)246-252
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume200
Issue number1
DOIs
Publication statusPublished - Apr 15 1994

Fingerprint

Biological membranes
Deuterium
Sarcoplasmic Reticulum
Stretching
Phospholipids
Rabbits
Membranes
Membrane structures
Hydrogenation
Infrared spectroscopy
Fourier transforms
Lipids
Atoms
Catalysts
Water
Fourier Analysis
Vibration
Spectrum Analysis
palladium sulfonated alizarine

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

In Situ Modification of the Phospholipid Environment of Native Rabbit Sarcoplasmic Reticulum Membranes. / Szalontai, B.; Vígh, L.; Joo, F.; Senak, L.; Mendelsohn, R.

In: Biochemical and Biophysical Research Communications, Vol. 200, No. 1, 15.04.1994, p. 246-252.

Research output: Contribution to journalArticle

@article{6aaea8bf327f417999a6d681e9b8c251,
title = "In Situ Modification of the Phospholipid Environment of Native Rabbit Sarcoplasmic Reticulum Membranes",
abstract = "A water soluble hydrogenation catalyst (palladium di(sodium alizarine monosulphonate)) in a deuterium-containing environment has been used for the in situ insertion of deuterium atoms into the fatty acyl chains of biological membranes. The thermotropic response of the stretching vibrations of the formed C-D bonds, as detected by Fourier transform IR spectroscopy, was used as a selective probe of biological membrane structure. Partial deuteration of unsaturated fatty acyl chains coupled with IR detection potentially provides a means for detecting specific biological roles of particular lipid classes. In the current study of sarcoplasmic reticulum membranes and purified phospholipid/CaATPase vesicles, it is also shown that νC-D monitors change at particular membrane locations which may remain undetected through the CH2 symmetric stretching frequency, a widely used IR spectral parameter. The latter reflects the average environment of the acyl chains. The approach described here may be suitable for wide applications to the study of biomembranes.",
author = "B. Szalontai and L. V{\'i}gh and F. Joo and L. Senak and R. Mendelsohn",
year = "1994",
month = "4",
day = "15",
doi = "10.1006/bbrc.1994.1441",
language = "English",
volume = "200",
pages = "246--252",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - In Situ Modification of the Phospholipid Environment of Native Rabbit Sarcoplasmic Reticulum Membranes

AU - Szalontai, B.

AU - Vígh, L.

AU - Joo, F.

AU - Senak, L.

AU - Mendelsohn, R.

PY - 1994/4/15

Y1 - 1994/4/15

N2 - A water soluble hydrogenation catalyst (palladium di(sodium alizarine monosulphonate)) in a deuterium-containing environment has been used for the in situ insertion of deuterium atoms into the fatty acyl chains of biological membranes. The thermotropic response of the stretching vibrations of the formed C-D bonds, as detected by Fourier transform IR spectroscopy, was used as a selective probe of biological membrane structure. Partial deuteration of unsaturated fatty acyl chains coupled with IR detection potentially provides a means for detecting specific biological roles of particular lipid classes. In the current study of sarcoplasmic reticulum membranes and purified phospholipid/CaATPase vesicles, it is also shown that νC-D monitors change at particular membrane locations which may remain undetected through the CH2 symmetric stretching frequency, a widely used IR spectral parameter. The latter reflects the average environment of the acyl chains. The approach described here may be suitable for wide applications to the study of biomembranes.

AB - A water soluble hydrogenation catalyst (palladium di(sodium alizarine monosulphonate)) in a deuterium-containing environment has been used for the in situ insertion of deuterium atoms into the fatty acyl chains of biological membranes. The thermotropic response of the stretching vibrations of the formed C-D bonds, as detected by Fourier transform IR spectroscopy, was used as a selective probe of biological membrane structure. Partial deuteration of unsaturated fatty acyl chains coupled with IR detection potentially provides a means for detecting specific biological roles of particular lipid classes. In the current study of sarcoplasmic reticulum membranes and purified phospholipid/CaATPase vesicles, it is also shown that νC-D monitors change at particular membrane locations which may remain undetected through the CH2 symmetric stretching frequency, a widely used IR spectral parameter. The latter reflects the average environment of the acyl chains. The approach described here may be suitable for wide applications to the study of biomembranes.

UR - http://www.scopus.com/inward/record.url?scp=0028335705&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028335705&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1994.1441

DO - 10.1006/bbrc.1994.1441

M3 - Article

C2 - 8166693

AN - SCOPUS:0028335705

VL - 200

SP - 246

EP - 252

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -