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Structural characterization of bovine CD36 from the milk fat globule membrane.
Department of Molecular Biology, University of Aarhus, Denmark.
Bovine CD36 from milk fat globule membranes was characterized and a full-length CD36 cDNA of 2772 nucleotides was isolated from a bovine mammary gland cDNA library. The deduced protein sequence contains 472 amino acid residues with 82-84% identity to the amino acid sequences of CD36 from other species. Peptides corresponding to 43% of the protein were sequenced. All eight potential N-glycosylation sites were glycosylated and the carbohydrate compositions of the individual sites were determined.
PMID: 8950178 [PubMed - indexed for MEDLINE]
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Cited by 1 PubMed Central article
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Cd36, a class B scavenger receptor, functions as a monomer to bind acetylated and oxidized low-density lipoproteins.
Martin CA, Longman E, Wooding C, Hoosdally SJ, Ali S, Aitman TJ, Gutmann DA, Freemont PS, Byrne B, Linton KJ.
Protein Sci. 2007 Nov; 16(11):2531-41. Epub 2007 Sep 28.
[Protein Sci. 2007]