Association of specific cell-surface glycoproteins with a triton X-100-resistant complex of plasma membrane proteins isolated from T-lymphoma cells (P1798)
|Published in||Experimental cell research. 1985, vol. 156, no. 1, p. 239-250|
|Abstract||A non-ionic detergent-resistant complex of membrane-associated proteins and cell-surface glycoproteins has been isolated by gel filtration and isopyknic centrifugation of purified plasma membranes from the murine T-lymphoma P 1798. This complex elutes as a high molecular weight peak (greater than 15 X 10(6) D) and contains two specific sets of (1) cell-surface glycoproteins; (2) membrane-associated proteins. The cell-surface glycoproteins consist of two vectorially labelled major components present in a fixed molar ratio: The Thy-1 glycoprotein and a non-H-2 glycoprotein of 55 kD. Minor but significant amounts of the class I histocompatibility antigen Qa-2 are also contained in the detergent-resistant complex. The membrane-associated proteins are not vectorially labelled, and form a complex group of proteins in the 30-70 kD range. Since actin is not detectable among these polypeptides, they probably constitute a plasma membrane-associated structure that is distinct from actin-containing, submembranous cytoskeletal elements.|
|Keywords||Animals — Cell Line — Cell Membrane/analysis — Detergents/ pharmacology — Electrophoresis, Polyacrylamide Gel — Glycoproteins/isolation & purification/ metabolism — Lymphoma/ pathology — Macromolecular Substances — Membrane Proteins/isolation & purification/ metabolism — Mice — Molecular Weight — Octoxynol — Polyethylene Glycols/ pharmacology — Surface-Active Agents/ pharmacology — T-Lymphocytes/ cytology|
This document has no fulltext available yet, but you can contact its author by using the form below.
|HOESSLI, Daniel, RUNGGER-BRANDLE, Elisabeth. Association of specific cell-surface glycoproteins with a triton X-100-resistant complex of plasma membrane proteins isolated from T-lymphoma cells (P1798). In: Experimental Cell Research, 1985, vol. 156, n° 1, p. 239-250. doi: 10.1016/0014-4827(85)90278-2 https://archive-ouverte.unige.ch/unige:10908|