Fatty acylation of a 55 kDa membrane protein of human erythrocytes

Das, Amit K. ; Kundu, Manikuntala ; Chakrabarti, Parul ; Basu, Joyoti (1992) Fatty acylation of a 55 kDa membrane protein of human erythrocytes Biochimica et Biophysica Acta (BBA) - Biomembranes, 1108 (2). pp. 128-132. ISSN 0005-2736

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000527...

Related URL: http://dx.doi.org/10.1016/0005-2736(92)90016-F

Abstract

The major palmitoylated human erythrocyte membrane protein has an Mr of 55000. It is distinct from the glucose transporter and is not derived from band 3 or ankyrin. It resists salt extraction suggesting a high affinity for the membrane. Pulse chase experiments demonstrate that palmitoylation is a dynamic process, and it may therefore have regulatory significance in membrane protein-protein or protein-lipid interaction. Slower dynamics of palmitoylation in erythrocytes from patients suffering from chronic myelogenous leukemia, which are less stable than normal erythrocytes, strenghten this view.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Membrane Protein; Palmitoylation; Chronic Myelogenous Leukemia; (Human Erythrocyte)
ID Code:1675
Deposited On:05 Oct 2010 09:48
Last Modified:17 Jan 2011 08:16

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