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An unusual form of lipid linkage to the CD45 peptide

Journal Article · · Science (Washington, D.C.); (USA)
;  [1]
  1. Brown Univ., Providence, RI (USA)
Some protein kinases and phosphatases are myristoylated on their amino terminus, which perhaps contributes to subcellular localization or regulation. Glycoprotein CD45, a hematopoietic tyrosine phosphatase, was examined for fatty acid content. The CD45 protein incorporated ({sup 3}H)myristate, but little ({sup 3}H)palmitate. The label was not metabolized and reincorporated into amino acids or saccharides, as revealed by peptide maps of CD45 labeled with ({sup 3}H)myristate, {sup 14}C-labeled amino acids, ({sup 35}S)methionine, or {sup 125}I, and glycosidase treatments, respectively. The myristate label was resistant to mild alkaline methanolysis and was found in fatty acid and sphingosine, indicating an unusual form of lipid attachment to CD45.
OSTI ID:
5962909
Journal Information:
Science (Washington, D.C.); (USA), Journal Name: Science (Washington, D.C.); (USA) Vol. 250:4981; ISSN SCIEA; ISSN 0036-8075
Country of Publication:
United States
Language:
English