Endosomal preparations from human osteosarcoma cells and from fibroblasts contain 51,000- and 26,000-Mr proteins which bind a small dermatan sulphate proteoglycan after SDS/polyacrylamide-gel electrophoresis and Western blotting. Binding can be inhibited by unlabelled proteoglycan core protein. The proteins co-precipitate with a proteoglycan core protein-antibody complex. Scatchard analysis of immobilized endosomal proteins yielded a KD of about 37 nM for the proteoglycan. In intact cells proteins of the same size can be found. They are sensitive to trypsinization. A 51,000-Mr protein is the predominant membrane protein with strong binding to immobilized dermatan sulphate proteoglycan. There are additional proteoglycan-binding proteins with Mr values of around 30,000 and 14,000 which are insensitive to trypsin treatment. In contrast with the 51,000- and 26,000-Mr proteins, they resist deoxycholate/Triton X-100 extraction several days after subcultivation.
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October 1989
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Research Article|
October 01 1989
Endocytosis of a small dermatan sulphate proteoglycan. Identification of binding proteins
H Hausser;
H Hausser
1Institute of Physiological Chemistry and Pathobiochemistry, University of Miinster, D-4400 Miinster, Federal Republic of Germany.
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W Hoppe;
W Hoppe
1Institute of Physiological Chemistry and Pathobiochemistry, University of Miinster, D-4400 Miinster, Federal Republic of Germany.
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U Rauch;
U Rauch
1Institute of Physiological Chemistry and Pathobiochemistry, University of Miinster, D-4400 Miinster, Federal Republic of Germany.
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H Kresse
H Kresse
1Institute of Physiological Chemistry and Pathobiochemistry, University of Miinster, D-4400 Miinster, Federal Republic of Germany.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1989 London: The Biochemical Society
1989
Biochem J (1989) 263 (1): 137–142.
Citation
H Hausser, W Hoppe, U Rauch, H Kresse; Endocytosis of a small dermatan sulphate proteoglycan. Identification of binding proteins. Biochem J 1 October 1989; 263 (1): 137–142. doi: https://doi.org/10.1042/bj2630137
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