Glycolipids are not extracted from phospholipid bilayers by binding to ferritin-lectin conjugates

Rhoderick E. Brown; Margaretta Allietta; Thomas W. Tillack; Thomas E. Thompson

doi:10.1016/0005-2736(83)90047-0

Glycolipids are not extracted from phospholipid bilayers by binding to ferritin-lectin conjugates

Rhoderick E. Brown
, Margaretta Allietta
, Thomas W. Tillack
, Thomas E. Thompson

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

A radioactively-labelled glycosphingolipid, asialo-G_M1, has been incorporated into phosphatidylcholine multilamellar vesicles. After incubation with ferritin-Ricinus communis agglutinin 60 (RCA 60) conjugate at different temperatures, the vesicles were separated from the conjugate by discontinuous density gradient ultracentrifugation. Measurement of the distribution of the radioactively-labelled asialo-G_M1 in the pelleted conjugate fraction and freeze-etch electron microscopy of the vesicle fraction indicate that the decrease in labelling of asialo-G_M₁-containing vesicles by ferritin-RCA 60 conjugate with increasing temperatures (Tillack, T.W., Wong, M., Allietta, M. and Thompson, T.E. (1982) Biochim. Biophys. Acta 691, 261-273) reflects a decrease in apparent binding affinity rather than an ability of the conjugate to extract glycolipid from the phospholipid bilayer after binding.

Original language	English (US)
Pages (from-to)	495-499
Number of pages	5
Journal	BBA - Biomembranes
Volume	731
Issue number	3
DOIs	https://doi.org/10.1016/0005-2736(83)90047-0
State	Published - Jun 23 1983
Externally published	Yes

Keywords

Electron microscopy
Ferritin-ricin conjugate
Freeze-etching
Glycosphingolipid anchoring
Phosphatidylcholine bilayer

Publisher link

10.1016/0005-2736(83)90047-0

Find It

Find It at U of M Libraries

Cite this

@article{c16b1d186e764235bef00295dd2249ea,

title = "Glycolipids are not extracted from phospholipid bilayers by binding to ferritin-lectin conjugates",

abstract = "A radioactively-labelled glycosphingolipid, asialo-GM1, has been incorporated into phosphatidylcholine multilamellar vesicles. After incubation with ferritin-Ricinus communis agglutinin 60 (RCA 60) conjugate at different temperatures, the vesicles were separated from the conjugate by discontinuous density gradient ultracentrifugation. Measurement of the distribution of the radioactively-labelled asialo-GM1 in the pelleted conjugate fraction and freeze-etch electron microscopy of the vesicle fraction indicate that the decrease in labelling of asialo-GM1-containing vesicles by ferritin-RCA 60 conjugate with increasing temperatures (Tillack, T.W., Wong, M., Allietta, M. and Thompson, T.E. (1982) Biochim. Biophys. Acta 691, 261-273) reflects a decrease in apparent binding affinity rather than an ability of the conjugate to extract glycolipid from the phospholipid bilayer after binding.",

keywords = "Electron microscopy, Ferritin-ricin conjugate, Freeze-etching, Glycosphingolipid anchoring, Phosphatidylcholine bilayer",

author = "Brown, \{Rhoderick E.\} and Margaretta Allietta and Tillack, \{Thomas W.\} and Thompson, \{Thomas E.\}",

year = "1983",

month = jun,

day = "23",

doi = "10.1016/0005-2736(83)90047-0",

language = "English (US)",

volume = "731",

pages = "495--499",

journal = "BBA - Biomembranes",

issn = "0005-2736",

publisher = "Elsevier B.V.",

number = "3",

}

TY - JOUR

T1 - Glycolipids are not extracted from phospholipid bilayers by binding to ferritin-lectin conjugates

AU - Brown, Rhoderick E.

AU - Allietta, Margaretta

AU - Tillack, Thomas W.

AU - Thompson, Thomas E.

PY - 1983/6/23

Y1 - 1983/6/23

N2 - A radioactively-labelled glycosphingolipid, asialo-GM1, has been incorporated into phosphatidylcholine multilamellar vesicles. After incubation with ferritin-Ricinus communis agglutinin 60 (RCA 60) conjugate at different temperatures, the vesicles were separated from the conjugate by discontinuous density gradient ultracentrifugation. Measurement of the distribution of the radioactively-labelled asialo-GM1 in the pelleted conjugate fraction and freeze-etch electron microscopy of the vesicle fraction indicate that the decrease in labelling of asialo-GM1-containing vesicles by ferritin-RCA 60 conjugate with increasing temperatures (Tillack, T.W., Wong, M., Allietta, M. and Thompson, T.E. (1982) Biochim. Biophys. Acta 691, 261-273) reflects a decrease in apparent binding affinity rather than an ability of the conjugate to extract glycolipid from the phospholipid bilayer after binding.

AB - A radioactively-labelled glycosphingolipid, asialo-GM1, has been incorporated into phosphatidylcholine multilamellar vesicles. After incubation with ferritin-Ricinus communis agglutinin 60 (RCA 60) conjugate at different temperatures, the vesicles were separated from the conjugate by discontinuous density gradient ultracentrifugation. Measurement of the distribution of the radioactively-labelled asialo-GM1 in the pelleted conjugate fraction and freeze-etch electron microscopy of the vesicle fraction indicate that the decrease in labelling of asialo-GM1-containing vesicles by ferritin-RCA 60 conjugate with increasing temperatures (Tillack, T.W., Wong, M., Allietta, M. and Thompson, T.E. (1982) Biochim. Biophys. Acta 691, 261-273) reflects a decrease in apparent binding affinity rather than an ability of the conjugate to extract glycolipid from the phospholipid bilayer after binding.

KW - Electron microscopy

KW - Ferritin-ricin conjugate

KW - Freeze-etching

KW - Glycosphingolipid anchoring

KW - Phosphatidylcholine bilayer

UR - https://www.scopus.com/pages/publications/25344433879

UR - https://www.scopus.com/pages/publications/25344433879#tab=citedBy

U2 - 10.1016/0005-2736(83)90047-0

DO - 10.1016/0005-2736(83)90047-0

M3 - Article

AN - SCOPUS:25344433879

SN - 0005-2736

VL - 731

SP - 495

EP - 499

JO - BBA - Biomembranes

JF - BBA - Biomembranes

IS - 3

ER -

Glycolipids are not extracted from phospholipid bilayers by binding to ferritin-lectin conjugates

Abstract

Keywords

Publisher link

Find It

Other files and links

Fingerprint

Cite this