The Journal of Antibiotics · 1986 · 53 citations · 9 references
Life SciencesBiochemistryMolecular BiologyDrug DiscoveryEnzymologyProtein BiochemistryAmino Acid ChemistryEnzyme DiscoveryEnzyme InhibitionPeptide ChemistryProtein ChemistryProteolytic EnzymesDipeptidyl PeptidasesPeptidase Activity
New aminopeptidase B inhibitors that we named OF4949-I, II, III and IV were isolated from the culture broth of a fungus, Penicillium rugulosum OF4949. The molecular formula of I was C23H26N4O8 and that of II, C22H24O8, judging from elemental analysis and secondary ion mass spectrometry. The concentrations of I, II, III and IV required for 50% inhibition of aminopeptidase, using Ehrlich ascites carcinoma cells as the source of the enzyme, were 0.0054, 0.0048, 3.4 and 1.7 micrograms/ml, respectively. Components I and II augmented delayed-type hypersensitivity in mice to sheep red blood cells.
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Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes.
HAMAO UMEZAWA, TAKAAKI AOYAGI, Suda Hiroyuki et al. · The Journal of Antibiotics · 1976 · 721 citations · Full text
Effect of bestatin on mouse immune system and experimental murine tumors.
Masaaki Ishizuka, Toru Masuda, NOBUO KANBAYASHI et al. · The Journal of Antibiotics · 1980 · 131 citations · Full text
Medicine, Immunology, Oncology +14