Open AccessIsolation of a specific granulopoiesis inhibitor from calf spleen and identification as glutathione
Author(s) -
FETSCH Jörg,
ECKART Klaus,
MAURER H. Rainer
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb19141.x
Subject(s) - granulopoiesis , isolation (microbiology) , spleen , glutathione , identification (biology) , biology , chemistry , haematopoiesis , immunology , biochemistry , microbiology and biotechnology , bioinformatics , stem cell , enzyme , botany
A small peptide was isolated from calf spleen, specifically inhibiting murine granulopoiesis in vitro . Purification involved ultrafiltration, anion‐exchange chromatography with a FPLC system and reversed‐phase chromatography on HPLC. Determination of the amino acid composition, following acid hydrolysis and phenyl isothiocyanate and dabsyl chloride derivatization, revealed the amino acids glutamic acid, cysteine and glycine. Although the N‐terminal amino group was not blocked, peptide sequencing with common techniques was not possible. Comparison of the isolated peptide with the well‐known tripeptide glutathione by HPLC and fast atom bombardment (FAB)/tandem mass spectrometry showed the identify of both substances. Moreover, glutathione was found to be a specific granulopoiesis inhibitor in vitro at 10–100 nM, a so far unknown property of this well‐known peptide.