ISSN:
1573-4919
Keywords:
prothymosin α
;
primary sequence
;
goat
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Abstract Goat prothymosin α, a highly acidic polypeptide of pl 3.5, 109 amino acid residues, has been isolated from lymphoid and non-lymphoid tissues of young female goats. Unlike rat, murine and porcine prothymosins α, goat prothymosin α appears at a higher concentration in the spleen compared with the thymus. The sequence of segments of the polypeptide involving known mutations has been determined, by automatic sequencing of its tryptic peptide fragments. The acidic amino acid-rich segment in the middle of the molecule, including residues 49–83, has not been sequenced. Goat prothymosin α closely resembles bovine prothymosin α, with only one substitution, proline for alanine at position 85. It also resembles human prothymosin α, with only three substitutions. It differs more significantly from rat and murine prothymosins α, by two deletions and three substitutions. The results show the highly conserved nature of the molecule, with substitutions at given positions only.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00239545
