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  • Title: Developmental regulation of pp44/46, tyrosine-phosphorylated proteins associated with tyrosine/serine kinase activity in Trypanosoma brucei.
    Author: Parsons M, Ledbetter JA, Schieven GL, Nel AE, Kanner SB.
    Journal: Mol Biochem Parasitol; 1994 Jan; 63(1):69-78. PubMed ID: 8183324.
    Abstract:
    The pattern of tyrosine-phosphorylated proteins is developmentally regulated in Trypanosoma brucei. To examine the function and regulation of these tyrosine-phosphorylated molecules, monoclonal antibodies were generated using purified tyrosine-phosphorylated proteins as immunogens. Two monoclonal antibodies were obtained. Both react with a set of proteins at 44-46 kDa, collectively referred to as pp44/46, that are phosphorylated on serine and tyrosine. Differentiation of the parasite from slender bloodforms to procyclic forms was accompanied by increased abundance and tyrosine-phosphorylation of pp44/46. The monoclonal antibodies immunoprecipitated protein kinase activity capable of phosphorylating pp44/46 on serine and tyrosine, and myelin basic protein on serine. The data indicate that the prominent tyrosine-phosphorylated proteins induced upon differentiation are either themselves protein kinases or that they are associated with protein kinases.
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