Polypeptide structure of human terminal transferase |
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Authors: | P Plevani L Capucci G Badaracco D Breviario N Sacchi G Cattoretti E Ginelli |
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Affiliation: | 1. Istituto di Biologia, Università di Milano and E.U.L.O., Brescia, Italy.;4. Istituto di Fisiologia Generale, Università di Genova, Italy.;1. Clinica Pediatrica, Università di Milano, Italy. |
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Abstract: | The polypeptide structure of terminal transferase purified from human lymphoblasts was examined with an immunoblot procedure using rabbit anti-calf thymus terminal transferase antibodies. Two doublets of bands of Mr 58-56,000 and Mr 44-42,000 are the major immunoreactive polypeptides. Only the Mr 44-42,000 polypeptides can be efficiently renatured after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Controlled degradation with trypsin produces fully active enzyme containing the α and β polypeptides typical of the low molecular weight terminal transferase, suggesting that the different forms of purified terminal transferase may arise by proteolysis of the Mr 58,000 polypeptide. |
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