Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by HANSSON, C. G.
Right arrow Articles by SAMUELSSON, B. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by HANSSON, C. G.
Right arrow Articles by SAMUELSSON, B. E.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1978, Vol. 83, No. 3 813-819
© 1978 Japanese Biochemical Society


research-article

The Identification of Sulphatides in Human Erythrocyte Membrance and Their Relation to Sodium-Potassium Dependent Adenosine Triphosphatase

C. Gunnar HANSSON, Karl-Anders KARLSSON and Bo E. SAMUELSSON

Department of Medical Biochemistry, University of Göteborg S-400 33 Göteborg 33, Sweden

Sulphatides (ceramide galactose-3-sulphate) were isolated from human erythrocyte membranes. The amount obtained was 3.3 mg from 6.7 kg of wet cells, or 1.5×10–9 mol per g dry cells. The polar part was shown to be galactose-3-sulphate by chromatographic analysis, infrared spectrometry, and mass spectrometry after solvolytic desulphation. The ceramide part consisted of three major molecular species, sphingosine-palmitic acid, sphingosine-2-hydroxy-palmitic acid, and phytosphingosine-2-hydroxypalmitic acid, as shown by thin-layer chromatography, mass spectrometry of galactosylceramides after desulphation, and gas chromatography of components after hydrolysis. The composition differed from other human erythrocyte sphingolipids.

Although the amount of sulphatides is very low for erythrocyte, the ratio of sulphatide concentration and Na+-K+-ATPase activity [EC 3.6.1.3 [EC] ] is similar to the situation found for several animal tissues with an increased level of Na+ transport. This finding is discussed in relation to a recent model of sulphatide function in a transport unit for Na+ and K+ (cofactor site model).


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Hum Mol GenetHome page
U. Matzner, E. Herbst, K. K. Hedayati, R. Lullmann-Rauch, C. Wessig, S. Schroder, C. Eistrup, C. Moller, J. Fogh, and V. Gieselmann
Enzyme replacement improves nervous system pathology and function in a mouse model for metachromatic leukodystrophy
Hum. Mol. Genet., May 1, 2005; 14(9): 1139 - 1152.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
G.A. Barabino, X.D. Liu, B.M. Ewenstein, and D.K. Kaul
Anionic Polysaccharides Inhibit Adhesion of Sickle Erythrocytes to the Vascular Endothelium and Result in Improved Hemodynamic Behavior
Blood, February 15, 1999; 93(4): 1422 - 1429.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.