Structural elucidation of alpha-MAPI, a novel microbial alkaline proteinase inhibitor, produced by Streptomyces nigrescens WT-27

✍ Scribed by Takashi Watanabe; Kenichi Fukuhara; Sawao Murao

• Book ID: 104237575
• Publisher: Elsevier Science
• Year: 1979
• Tongue: French
• Weight: 232 KB
• Volume: 20
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/s0040-4039(01)86020-2

✦ Synopsis

As reproted in previous papers [l, 21, a novel proteinase inhibitor MAPI, produced by streptomyces nigrescens WT-27, showed a specific inhibitory activity against various microbial alkaline proteinases, a-chymotrypsin and thiol proteinases. MAP1 in the culture filtrate was purified successively via adsorption on Amberlite XAD-2, extraction with n-butanol, chromatography using Amberlite XAD-7, Dowex 1X2, Amberlite CG-50, alumina and silica gel. MAPI was a mixture of three compounds (designated as c--, 8-, and y-MAPI), which showed the same inhibitory spectra but different inhibitory potentials. a-MAPI was isolated by preparative high performance liquid chromatography (HPLC) and crystallized from aqueous methanol as needles. Properties of c(-MAPI were as follows: mp 204s20S°C(dec.); [a];' -18O(c 1.0, acetic acid); Found: C 58.49, H 6.97, N 15.54%; Calcd. for C~OHI,~N~O~.HZO: C 58.71, H 7.06, N 15.98%; IR (KBr): 3400Q3300(NH), 1650c1640(amide I, guanidinium and ureido), 1550%1540(amide II), 1460%1440(phenyl), 1390(COOH), 750, 690cm-'(phenyl); UV: Amax 80%aq.MeOH(,) 268 (304), 264 (4021, 258(509), 252(440), 247m(360); PMR[9ObfHz, d value(ppm) in DMF-d71: