• Subhash Basu

      Articles written in Journal of Biosciences

    • The role of eucaryotic cell surface glycoconjugates in DNA replication

      Subhash Basu Prabir Bhattacharya Manju Basu

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      Multiple forms of ricin have been isolated from castor bean seeds. Two forms, ricin-1 and ricin-2, differ in their isoelectric pI values and toxicity towards IMR-32 cells. Inhibition of IMR-32 DNA polymerase α2 is more pronounced with ricin-1 (65%) than with ricin-2 (10%). Ricin B chain (pI = 5.2) isolated from ricin-1 binds to IMR-32 cell surfaces as well as inhibits DNA polymerase α2 activity when studiedin vitro. The presence of galβ-linked glycoconjugates near the active site of IMR-32 DNA polymerase α2 has been proposed. Replication modulators which bind to the glycose portion of the enzymes involved in the replication system may need a mandatory binding to cell surface glycoconjugates for their activity.

    • Biosynthesis of eukaryotic cell surface glycosphingolipids using solubilized glycosyltransferases

      Subhash Basu Tripti De John W Kyle Manju Basu

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      Two fucsyltransferases (FucT-2 and FucT-3) have been solubilized from Golgi-rich membrane fraction of bovine spleen, using a cationic detergent. FucT-3 was distinguished from FucT-2 by comparing their kinetic parameters and heat stability. FucT-2 and FucT-3 lost activity (85 %) and (5 %), respectively, when heated at 55°C for 10 sec. Two galactosyltransferases (GalT-3 and GalT-4) and two sialyltransferases (SAT-2 and SAT-3) have also been solubilized from embryonic chicken brain membranes using nonionic detergents. Affinity chromatography and microisoelectric focusing were used to separate these enzymes into functionally pure fractions. Anomeric and positional linkages in some of the products (LM1 and LD1c) have also been established. The terminal NeuAc(α2-8) linkage in GD3 and LD1c was established by identification of the partially methylated penultimate [Ac-14C]sialic acid.

    • Resolution of DNA polymerase-α-primase complex and primase free

      Ira Simet Satyajit Ray Subhash Basu

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      DNA Polymerase-α from embryonic chicken brain was resolved on DEAE-cellulose into 3 comPonent activities that remained distinct uPon rechromatograPhy. Product formation by each activity required exogenously added temPlate-Primer DNA, all 4 deoxynucleoside triPhosPhates, and a divalent metal cation. Each form incorPorated [3H]-dTTP or [3H]-dCTP into a high molecular weight Product that was identified as DNA by its chromatograPhic behavior and its sensitivity to DNase. High ionic strength, N-ethylmaleimide, and the Polymerase-α-sPecific inhibitor aPhidicolin inhibited each activity; the aPParentKi value of aPhidicolin was 3.0 μM in each case. Based on these results, the 3 activities were identified as multiPle forms of DNA Polymerase-α . ExPeriments using embryonic chicken brains of various ages indicated that Polymerase-α1, and Polymerase-α3 reached maximal activity in 9-day-old embryos, while Polymerase-α2 activity was elevated at a slightly later develoPmental stage. Using Poly (dC) as temPlate, high Primase activity was detected in Polymerase-α1, fractions.

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