Lentil Lectin Enriched Microsomes from the Plasma Membrane of the Human B-Lymphocyte Cell Line H2LCL Carry a Heavy Load of Type-1 Porin
Using an established biochemical approach, five subcellular fractions of human B lymphocytes were prepared by differential centrifugation. Crude membranes were passed over a lentil lectin column to enrich carbohydrate-coated cell surface microsomes. The lectin-bound fraction contained a high amount...
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Published in | Biological chemistry Vol. 379; no. 12; pp. 1419 - 1426 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
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Berlin, New York
Walter de Gruyter, Berlin / New York
01.12.1998
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Abstract | Using an established biochemical approach, five subcellular fractions of human B lymphocytes were prepared by differential centrifugation. Crude membranes were passed over a lentil lectin column to enrich carbohydrate-coated cell surface microsomes. The lectin-bound fraction contained a high amount of plasma membrane-derived microsomes as indicated by cell surface markers. All subcellular fractions in Western blots proved to contain distinct but variable amounts of porin. There was a strong increase in porin content from crude membranes to plasma membrane-derived vesicles. The porin content of this fraction appeared to be higher than that of mitochondria. In the final step the plasma membrane-derived microsome fraction proved to be devoid of contamination by outer mitochondrial membranes, as revealed by antibodies against the established markers MAO B and Tom20 applied in Western blots. These data prove the extramitochondrial expression of human type-1 porin/ type-1 VDAC. |
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AbstractList | Using an established biochemical approach, five subcellular fractions of human B lymphocytes were prepared by differential centrifugation. Crude membranes were passed over a lentil lectin column to enrich carbohydrate-coated cell surface microsomes. The lectin-bound fraction contained a high amount of plasma membrane-derived microsomes as indicated by cell surface markers. All subcellular fractions in Western blots proved to contain distinct but variable amounts of porin. There was a strong increase in porin content from crude membranes to plasma membrane-derived vesicles. The porin content of this fraction appeared to be higher than that of mitochondria. In the final step the plasma membrane-derived microsome fraction proved to be devoid of contamination by outer mitochondrial membranes, as revealed by antibodies against the established markers MAO B and Tom20 applied in Western blots. These data prove the extramitochondrial expression of human type-1 porin/ type-1 VDAC. |
Author | Hellmann, Klaus P. Awni, Lewa A. Hellmann, Thea Kleineke, Jochen Götz, Hilde Reymann, Susanne Paetzold, Gabriele Eben-Brunnen, Jana Thinnes, Friedrich P. Cole, Thomas Hilschmann, Norbert |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9894809$$D View this record in MEDLINE/PubMed |
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SubjectTerms | B-Lymphocytes - metabolism Blotting, Western Cell Compartmentation Cell Line, Transformed Chromatography, Affinity Electrophoresis, Polyacrylamide Gel Enzyme-Linked Immunosorbent Assay Humans Lectins - administration & dosage Microsomes - metabolism Plant Lectins Porins - metabolism |
Title | Lentil Lectin Enriched Microsomes from the Plasma Membrane of the Human B-Lymphocyte Cell Line H2LCL Carry a Heavy Load of Type-1 Porin |
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