Bovine parathymosin: amino acid sequence and comparison with rat parathymosin

C Panneerselvam, M Clinton, D Wellner, B L Horecker

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Parathymosin has been purified from calf liver and its primary sequence established, except for a segment containing approximately 11 amino acid residues in the central part of the polypeptide chain. Bovine parathymosin contains approximately 101 amino acid residues and shows 90% identity with rat parathymosin, with substitution of Glu for Asp at positions 21, 57, and 58, Asp for Glu at positions 60 and 63, and Ala for Val at position 77. Three non-conservative substitutions were Ala for Thr at position 81, Leu for Arg at position 78, and Val for Lys at position 79. The replacement at the last two positions of a pair of basic by hydrophobic amino acid residues may account for differences in chromatographic behavior observed for the bovine and rat polypeptides. Analysis of the NH2-terminus employed a new deblocking procedure which was also employed to analyze rat parathymosin, requiring correction of the previously published NH2-terminal sequence for that polypeptide.
Original languageEnglish
Pages (from-to)539-45
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 1988


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