Premium
SOME PHYSICOCHEMICAL PROPERTIES OF HUMAN LEUCOCYTE MIGRATION INHIBITORY FACTOR (LIF)
Author(s) -
BENDTZEN K.
Publication year - 1976
Publication title -
acta pathologica microbiologica scandinavica section c immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0304-1328
DOI - 10.1111/j.1699-0463.1976.tb00057.x
Subject(s) - pmsf , chemistry , sodium fluoride , ethanol , concanavalin a , esterase , dodecylbenzene , fluoride , biochemistry , enzyme , sodium , stereochemistry , in vitro , organic chemistry , sulfonate , inorganic chemistry
Leucocyte migration inhibitory factor (LIF) obtained from human lymphocytes stimulated with concanavalin A was consistently and irreversibly blocked by the serine‐esterase inhibitor phenyl‐methyl sulphonylfluoride (PMSF). This effect was not due to fluoride ions, hydrolysis products of PMSF or to impurities. PMSF pulse treatment of human buffy coat cells did not affect cell migration under agarose. LIF was also irreversibly destroyed by treatment with L‐cysteine and 2‐mercapto‐ethanol, suggesting that the molecule contains disulphide linkage groups decisive for its configuration and biological activity. Di‐sodium EDTA completely inhibited LIF activity but only if present during the entire migration period. Removal of EDTA before LIF assay restored LIF activity. Leucocyte migration was neither influenced by L‐cysteine nor by EDTA. LIF activity was slightly diminished after treatment at 56°C for 1 h and completely lost at 80°C for /a h. Furthermore, LIF appeared rather stable when treated at pH values between 4 and 11. These findings suggest, but do not prove, an esterase or a protease nature of human LIF.