Isolation and partial characterization of prothymosin α from porcine tissues

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...

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Bibliographic Details
Published in:FEBS letters 1988-06, Vol.233 (2), p.342-346
Main Authors: Economou, M., Seferiadis, K., Frangou-Lazaridis, M., Horecker, B.L., Tsolas, O.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Aminoacids, peptides. Hormones. Neuropeptides
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Chromatography, Gel
Chromatography, High Pressure Liquid
Fundamental and applied biological sciences. Psychology
high-pressure liquid chromatography
HPLC
Humans
Isoelectric Focusing
Kidney - analysis
Lung - analysis
Male
mixed lymphocyte response
MLR
Molecular Sequence Data
Organ Specificity
Peptide Fragments - isolation & purification
pigs
Protein Precursors - isolation & purification
Proteins
prothymosin alpha
Prothymosin α
ProTα
Rats
Species Specificity
Spleen - analysis
Swine
Thymic peptide
Thymosin - analogs & derivatives
Thymosin - isolation & purification
Thymus Gland - analysis
Trypsin
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Description
Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)80456-3