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An extracellular protease was identified fromBacilus subtilis KCCM 10257 by N-terminal sequencing andmas spectral analysis. The molecular mas of the extracellularprotease was estimated to be 28 kDa by SDS-PAGE. Sequencingof the N-terminal of the protease revealed the sequence ofA(G,S,R)QXVPYG(A)V(P,L)SQ. The N-terminal sequenceexhibited close similarity to the sequence of other proteasesfrom Bacilus sp. A mass list of the monoisotopic peaks in theMALDI-TOF spectrum was searched after peptide fragmentationof the protease. Six peptide sequences exhibiting monoisotopic1,03.46 were observed from the fragmented protease. Thesemonisotopic masses coresponded to the lytic enzyme L27from Bacillus subtilis 168, and the Mowse score was found tobe 75. A doubly charged Top product (MS) at a m/z of 517.3exhibiting a molecular mass of 1034.6 was further analyzedby de novo sequencing using a PE Sciex QSTAR HybridQuadropole-TOF (MS/MS) mass spectrometer. MS/MS spectraof the Top product (MS) at a m/z of 517.3 obtained from thethe b-ion series of 114.2, 171.2, 286.2, 357.2, 504.2, 667.4, 830.1,and 887.1 and y-ion series of 147.5, 204.2, 367.2, 530.3,677.4, 748.4, 863.4, and 920.5. The sequence of analyzedpeptide ion was identified as LGDAFYYG from the b- and y-ionseries by de novo sequencing and corresponded to the results fromthe MALDI-TOF spectrum. From these results the extracellularprotease from Bacillus subtilis KCCM 10257 was successfullyidentified with the lytic enzyme L27 from Bacillus subtilis 168.

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참고문헌 (33건) : 자료제공( 네이버학술정보 )

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번호 참고문헌 국회도서관 소장유무
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