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 in situ 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.
Polypeptide structure of human terminal transferase / P. Plevani, L. Capucci, G. Badaracco, D. Breviario, N. Sacchi, G. Cattoretti, E. Ginelli. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - 108:3(1982 Oct 15), pp. 1196-203-1203.
Polypeptide structure of human terminal transferase
P. PlevaniPrimo
;N. Sacchi;E. GinelliUltimo
1982
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 in situ 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.Pubblicazioni consigliate
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