Premium
Human Leukocyte Migration Inhibitory Factor (LIF)
Author(s) -
BENDTZEN K.
Publication year - 1977
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1977.tb00341.x
Subject(s) - phenylmethylsulfonyl fluoride , pmsf , serine protease , protease , chemistry , tosyl , enzyme , serine , esterase , arginine , biochemistry , stereochemistry , amino acid
Previous findings suggesting an esterase and protease nature of human leukocyte migration inhibitory factor (LIF) were extended by testing the ability of different protease and esterase inhibitors to reduce LIF activity. The serine‐specific inhibitors phenylmethylsulfonyl fluoride (PMSF) and physostigmine (eserine) markedly reduced LIF activity, whereas the histidine‐specific inhibitors N ‐tosyl‐L‐lysine chloromethyl ketone (TLCK) and L‐tosylamide‐2‐phenylethyl chloromethyl ketone (TPCK) were inactive. That LIF might act as an esterase and a protease was further strengthened by the ability of pralidoxime methansulfonate (2‐PAM) to reestablish LIF activity of supernatants previously inactivated by PMSF. Furthermore, the arginine amides N ‐benzoyl‐L‐arginine‐ p ‐nitroanilide (BApNA) and N ‐benzoyl‐L‐phenylalanyl‐L‐valyl‐L‐arginine‐ p ‐nitroanilide (BPVApNA) were shown to satisfy the substrate specificities of the putative LIF enzyme. Indeed, BPVApNA seemed to possess a particularly strong affinity for LIF, indicating its potential role in an enzymatic LIF assay.