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Isolation and partial characterization of prothymosin α from porcine tissues
Author(s) -
Economou M.,
Seferiadis K.,
Frangou-Lazaridis M.,
Horecker B.L.,
Tsolas O.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80456-3
Subject(s) - amino acid , biochemistry , aspartic acid , glutamic acid , chemistry , peptide sequence , spleen , biology , microbiology and biotechnology , gene , immunology
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.