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Solid‐phase synthesis of biologically active fragment 29–111 of rat prothymosin alpha
Author(s) -
Abiko T.,
Sekino H.
Publication year - 1991
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1991.tb00161.x
Subject(s) - thymosin , peptide , chemistry , size exclusion chromatography , residue (chemistry) , chromatography , hydrogen fluoride , alpha (finance) , stereochemistry , biochemistry , enzyme , organic chemistry , medicine , construct validity , nursing , patient satisfaction
Rat prothymosin alpha fragment 29–111, an 83‐residue polypeptide corresponding to desthymosin alpha 1‐prothymosin alpha, has been synthesized by a solid‐phase method. Hydrogen fluoride was used to deprotect and cleave the peptide from the resin. The crude product was purified by gel‐filtration, ion‐exchange chromatography and high‐performance liquid chromatography. A 3.2‐mg sample of a ca. 96% pure peptide was finally obtained. The overall yield of the synthesis was less than 1%. An increase of E‐rosette‐forming lymphocytes was obtained after incubation of peripheral blood from uremic patients with the synthetic prothymosin alpha fragment 29–111. The restoring effect of the synthetic prothymosin alpha fragment 29–111 was greater than that of our synthetic thymosin alpha 1.