Proton Magnetic Resonance Studies of Whole Human Erythrocyte Membranes

Michael Sheetz, Sunney I. Chan

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

An analysis of the proton magnetic resonance (pmr) spectra of human erythrocyte membranes has been made in terms of the membrane components. The spectrum at 75° was assigned to 20% of the membrane proteins, 20% of the choline methyl groups of the phospholipids, and the acetamide groups of the sugars. Changes in the pmr spectra were noted when the membranes were altered by either protein solubilization or membrane fragmentation. The choline methyl signal was found to be particularly sensitive to the state of the membranes. Certain proteins were found to be released from the membranes at high temperatures and this phenomenon was dependent upon the pH and the solvent, as well as the presence of certain ions in solution. The amount of proteins solubilized, however, was significantly less than that observed by the high-resolution pmr method. The effect of certain divalent ions was particularly striking. The presence of more than 5 X 10-4m Mg2+for example, was sufficient to stabilize the proteins in the membrane and eliminate the high-resolution pmr signal.

Original languageEnglish (US)
Pages (from-to)548-555
Number of pages8
JournalBiochemistry
Volume11
Issue number4
DOIs
StatePublished - Feb 1 1972
Externally publishedYes

Fingerprint

Erythrocyte Membrane
Protons
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Membranes
Choline
Membrane Proteins
Ions
Proteins
Phospholipids
Sugars
Temperature

ASJC Scopus subject areas

  • Biochemistry

Cite this

Proton Magnetic Resonance Studies of Whole Human Erythrocyte Membranes. / Sheetz, Michael; Chan, Sunney I.

In: Biochemistry, Vol. 11, No. 4, 01.02.1972, p. 548-555.

Research output: Contribution to journalArticle

@article{c8bee9137f8f41d4bcd93a5422c5a07b,
title = "Proton Magnetic Resonance Studies of Whole Human Erythrocyte Membranes",
abstract = "An analysis of the proton magnetic resonance (pmr) spectra of human erythrocyte membranes has been made in terms of the membrane components. The spectrum at 75° was assigned to 20{\%} of the membrane proteins, 20{\%} of the choline methyl groups of the phospholipids, and the acetamide groups of the sugars. Changes in the pmr spectra were noted when the membranes were altered by either protein solubilization or membrane fragmentation. The choline methyl signal was found to be particularly sensitive to the state of the membranes. Certain proteins were found to be released from the membranes at high temperatures and this phenomenon was dependent upon the pH and the solvent, as well as the presence of certain ions in solution. The amount of proteins solubilized, however, was significantly less than that observed by the high-resolution pmr method. The effect of certain divalent ions was particularly striking. The presence of more than 5 X 10-4m Mg2+for example, was sufficient to stabilize the proteins in the membrane and eliminate the high-resolution pmr signal.",
author = "Michael Sheetz and Chan, {Sunney I.}",
year = "1972",
month = "2",
day = "1",
doi = "10.1021/bi00754a011",
language = "English (US)",
volume = "11",
pages = "548--555",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "4",

}

TY - JOUR

T1 - Proton Magnetic Resonance Studies of Whole Human Erythrocyte Membranes

AU - Sheetz, Michael

AU - Chan, Sunney I.

PY - 1972/2/1

Y1 - 1972/2/1

N2 - An analysis of the proton magnetic resonance (pmr) spectra of human erythrocyte membranes has been made in terms of the membrane components. The spectrum at 75° was assigned to 20% of the membrane proteins, 20% of the choline methyl groups of the phospholipids, and the acetamide groups of the sugars. Changes in the pmr spectra were noted when the membranes were altered by either protein solubilization or membrane fragmentation. The choline methyl signal was found to be particularly sensitive to the state of the membranes. Certain proteins were found to be released from the membranes at high temperatures and this phenomenon was dependent upon the pH and the solvent, as well as the presence of certain ions in solution. The amount of proteins solubilized, however, was significantly less than that observed by the high-resolution pmr method. The effect of certain divalent ions was particularly striking. The presence of more than 5 X 10-4m Mg2+for example, was sufficient to stabilize the proteins in the membrane and eliminate the high-resolution pmr signal.

AB - An analysis of the proton magnetic resonance (pmr) spectra of human erythrocyte membranes has been made in terms of the membrane components. The spectrum at 75° was assigned to 20% of the membrane proteins, 20% of the choline methyl groups of the phospholipids, and the acetamide groups of the sugars. Changes in the pmr spectra were noted when the membranes were altered by either protein solubilization or membrane fragmentation. The choline methyl signal was found to be particularly sensitive to the state of the membranes. Certain proteins were found to be released from the membranes at high temperatures and this phenomenon was dependent upon the pH and the solvent, as well as the presence of certain ions in solution. The amount of proteins solubilized, however, was significantly less than that observed by the high-resolution pmr method. The effect of certain divalent ions was particularly striking. The presence of more than 5 X 10-4m Mg2+for example, was sufficient to stabilize the proteins in the membrane and eliminate the high-resolution pmr signal.

UR - http://www.scopus.com/inward/record.url?scp=0015507318&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0015507318&partnerID=8YFLogxK

U2 - 10.1021/bi00754a011

DO - 10.1021/bi00754a011

M3 - Article

VL - 11

SP - 548

EP - 555

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 4

ER -