Isolation and partial characterization of prothymosin alpha from porcine tissues.
Prothymosin alpha, 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 alpha yielded peptides which on separation, amino acid analysis and alignment with the known sequence of prothymosin alpha from rat and man showed that the amino terminal portion of the molecule is conserved and the few differences present are confined to the carboxy terminal.
Economou
M
M
Laboratory of Biological Chemistry, University of Ioannina Medical School, Greece.
Seferiadis
K
K
Frangou-Lazaridis
M
M
Horecker
B L
BL
Tsolas
O
O
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D007525:Isoelectric Focusing; D007668:Kidney / Q000032:analysis; D008168:Lung / Q000032:analysis; D008297:Male; D008969:Molecular Sequence Data; D009928:Organ Specificity; D010446:Peptide Fragments / Q000302:isolation & purification; D011498:Protein Precursors / Q000302:isolation & purification; D051381:Rats; D013045:Species Specificity; D013154:Spleen / Q000032:analysis; D013552:Swine; D013947:Thymosin / Q000031:analogs & derivatives* / Q000302:isolation & purification; D013950:Thymus Gland / Q000032:analysis; D014357:Trypsin
D010446:Peptide Fragments; D011498:Protein Precursors; C040782:prothymosin alpha; D013947:Thymosin; D014357:Trypsin