@article{oai:oacis.repo.nii.ac.jp:00002354,
 author = {Kobayashi, Takeshi and Nakagawa, Naoji and Imada, Chiaki and 佐藤, 奈保子 and サトウ, ナオコ and Hamada, Naoko and 濱田, 奈保子},
 issue = {2},
 journal = {Fisheries Science},
 month = {Apr},
 note = {The extracellular production of a thermolysin inhibitor by 534 wild-type strains isolated from marine sediments and related-type strains was examined. The inhibition of thermolysin activity by strain T-177 was observed on a casein agar medium. According to our detailed taxonomic study, strain T-177 is related to Brevibacillus laterosporus. Further screening for a thermolysin inhibitor was performed using strain T-177 and nine other taxonomically related Brevibacillus type strains, and the ability to produce the inhibitor was observed in five strains. Among these strains, B. reuszeri IFO 15719^T exhibited the highest thermolysin inhibitory activity in broth media, and thus was used for the purification and characterization of the inhibitor. Chromatographic analyses suggested that this substance is a monomeric protein with a molecular mass of 60 kDa.},
 pages = {299--305},
 title = {Occurrence of a metalloprotease (thermolysin) inhibitor among Brevibacillus species and purification of such inhibitor from Brevibacillus reuszeri IFO 15719^T},
 volume = {70},
 year = {2004},
 yomi = {ハマダ, ナオコ}
}