Isolation and partial characterization of prothymosin α from porcine tissues

FEBS Letters

Seferiadis, K.¹  Tsolas, O.¹  Frangou-Lazaridis, M.¹  Horecker, B.L.²  Economou, M.¹ 

[1] Laboratory of Biological Chemistry, University of Ioannina Medical School, GR-453 32 Ioannina, Greece;Department of Biochemistry, Cornell University Medical College, New York, NY 10021, USA

关键词: Prothymosin α;    Thymic peptide;    ProTα;    prothymosin α;    HPLC;    high-pressure liquid chromatography;    MLR;    mixed lymphocyte response;   

DOI  :  10.1016/0014-5793(88)80456-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Prothymosin α, an immunoactive polypeptide of 12 kDa, has been isolated from porcine thymus, spleen, lung and kidney. It lacks aromatic and sulfur-containing amino acids and has a high content of glutamic and aspartic acids. Tryptic digestion of porcine thymus prothymosin α yielded peptides which on separation, amino acid analysis and alignment with the known sequence of prothymosin α from rat and man showed that the amino terminal portion of the molecule is conserved and the few differences present are confined to the car☐y terminal.

【 授权许可】

Unknown