Extracellular serine-proteinases isolated from Streptomyces alboniger: Partial characterization and effect of aprotinin on cellular structure

作者：Lopes A; Coelho RRR; Meirelles MNL; Branquinha MH; Vermelho AB^*

来源：Memorias do Instituto Oswaldo Cruz, 1999, 94(6): 763-770.

DOI：10.1590/s0074-02761999000600010

• Streptomyces alboniger
• serine-proteinases
• growth
• aprotinin

Streptomyces alboniger ATCC 12461 grown in brain heart infusion (BHI) medium produced two extracelluar serine-proteinases, denoted SP I and SP II, which were purified by ammonium sulfate precipitation and aprotinin-agarose affinity chromatography. SP I was purified 88,9-fold and SP II 66, 7-fold, with 33.4% and 10.4% yield, respectively. The optinzum pH for the proteinases activity using alpha-N-p-tosyl-L-arginine-methyl ester (TAME) as substrate, was 9-10 and the optimum temperature was 37 degrees C. The proteolytic activity of SP I and SP II was inhibited by aprotinin and SP I was partially inhibited by leupeptin, both serine-proteinase inhibitors. S. alboniger growth in BHI-liquid medium decreased when 5 mu g/ml, 10 mu g/ml of a protinin was used being completely inhibited with 20 mu g/ml and 40 mu g/ml. At the ultrastructural level, aprotinin-treated S, alboniger cells showed swelling of the bacterial body and condensation of the genetic material, probably related to the inhibition of its growth.

• 出版日期1999-12