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학술저널
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한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제16권 제2호
발행연도
2006.1
수록면
264 - 271 (8page)

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Two fibrinolytic enzymes were purified from theculture supernatant of Fomitella fraxinea mycelia by ion-exchange and gel filtration chromatographies, and were designatedas F. fraxenia proteases 1 and 2 (FP1 and FFP2). The apparentmolecular mases of the enzymes were estimated to be 32 kDaand 42 kDa, respectively, by SDS-PAGE and gel filtrationchromatography. Both enzymes had the same optimal temperature(40oFFP2, respectively). FFP1 was relatively stable at pH 7.0-9.0and temperature below 30oC, whereas FFP2 was very stablein the pH range of 4-1 and temperature below 40oC. FFP1activity was completely inhibited by phenylmethylsulfonylfluoride (PMSF) and aprotinin, indicating that this enzyme isa serine protease. The activity of FFP2 was enhanced by theaddition of Co2+ and Zn2+ and inhibited by Cu2+, Ni2+, and Hg2+.Furthermore, FFP2 activity was strongly inhibited by EDTAand 1,10-phenanthroline, implying that the enzyme is ametalloprotease. Both enzymes readily hydrolyzed fibrinogen,preferentially digesting the Aα- and Bβ-chains of fibrinogenover γ-chain. FFP1 showed broad substrate specificity forsynthetic substrates, but FFP2 did not. Km and Vmax values ofFFP1 for a synthetic substrate, N-succinyl-Ala-Ala-Pro-Phe-pNA,amino acids of the N-terminal sequences of both enzymes wereAPXXPXGPWGPQRIS and ARPP(G)VDGQ(R,I)SK(L)ETLPE,respectively.

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