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  • Title: Two-dimensional analysis of metabolically and cell surface radiolabeled proteins of some human lymphoid and myeloid leukemia cell lines. II. Glycosylated and phosphorylated proteins.
    Author: Chorváth B, Duraj J, Sedlák J, Plesková I.
    Journal: Neoplasma; 1986; 33(5):565-70. PubMed ID: 3466044.
    Abstract:
    Cell surface glycoproteins, radiolabeled by sodium metaperiodate/tritiated borohydride technique and cell phosphoproteins, metabolically radiolabeled by 32P-orthophosphate were analyzed by two-dimensional electrophoretic analysis in some myeloid and lymphoid leukemia cell lines. Some markedly expressed major glycoproteins were predominant in some of cell lines (such as 95k and 100k glycoproteins with marked charge heterogeneity in non-T, non-B acute lymphoblastic leukemia cell lines NALM 6 and NALM 16), but markedly quantitatively reduced in other examined cell line, such as lymphoblastoid cell line UHKT 34/2. 32P-orthophosphate radiolabeled phosphoprotein two-dimensional patterns of examined lymphoid leukemia cell lines were essentially similar, with some minor differences, in examined lymphoid and myeloid leukemia cell lines, such as marked expression of a series of large phosphoproteins in the molecular weight range 80-100k in lymphoid cell lines and almost complete absence of these phosphoproteins on examined myeloid leukemia cell lines. Another configuration of acidic phosphoproteins (30-35k) exhibited individual cell line variability and differences between both individual myeloid leukemia cell lines and between lymphoid and myeloid cel lines examined.
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