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- Title
Human Leukocyte Migration Inhibitory Factor (LIF) III. Further Investigations on the Serine Protease Nature of This Lymphokine and Its Preference for Arginine Amides.
- Authors
Bendtzen, K.
- Abstract
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 LIP activity. The serine-specific inhibitors phenylmethylsulfonyl fluoride (PMSF) and physostigmine (eserine) markedly reduced LIP activity, whereas the histidine-specific inhibitors N-tosyl-L-lysine chloromethyl ketone (TLCK) and L-tosylamide-2-phenylethyl chloro-methyl 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 LIP activity of supernatants previously inactivated by PMSF. Furthermore, the arginine amides N-benzoyl-L-arginine-p-nitro-anilide (BApNA) and N-benzoyl-L-phenylalanyl-L-valyl-L-arginine-p-nitroanilide (BPVApNA) were shown to satisfy the substrate specificities of the putative LIP enzyme. Indeed, BPVApNA seemed to possess a particularly strong affinity for LIP, indicating its potential role in an enzymatic LIF assay.
- Subjects
LEUCOCYTES; ESTERASES; PROTEOLYTIC enzymes; ARGININE; AMIDES; LYMPHOKINES
- Publication
Scandinavian Journal of Immunology, 1977, Vol 6, Issue 10, p1055
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1977.tb00341.x