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- W4256114911 abstract "This chapter focuses on chondroadherin, which is a leucine-rich glycoprotein isolated from cartilage. It is another member of the family of proteins that contain leucine-rich repeats. It has been shown to be as potent as collagen type II and fibronectin in mediating cell attachment of chondrocytes to plastic. Although it does not promote cell spreading, its exact function remains to be resolved. Chondroadherin exists in two major isoforms, one with a calculated molecular weight of 38,353 and a pI of 9.76 and the other with a molecular weight of 37,304 and a pI of 9.5. The principal feature of the protein chain is a series of 10 leucine-rich repeats, the most of the N-terminal of which contains a free cysteine. The majority of chondroadherin is monomeric. The gene structure and the functional sites of chondroadherin are discussed in the chapter." @default.
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- W4256114911 date "1998-01-01" @default.
- W4256114911 modified "2023-10-18" @default.
- W4256114911 title "Chondroadherin 38 kDa leucine protein, 36 kDa" @default.
- W4256114911 doi "https://doi.org/10.1016/b978-012068911-8/50105-6" @default.
- W4256114911 hasPublicationYear "1998" @default.
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