Isolation and characterization of bacteriolytic enzyme from a marine bacterium Alteromonas sp. No.8-R
1995
Takamoto, S. (Hokkaido Univ., Hakodate (Japan). Faculty of Fisheries) | Yamada, K. | Ezura, Y.
Bacteriolytic enzymes produced by Alteromonas sp. No.8-R in nutrient broth were purified by ultrafiltration, ammonium sulfate precipitation, gel filtration, and cation-exchange chromatography. The bacteriolytic fractions after gel filtration contained six protein bands (A to F) on polyacrylamide gel electrophoresis (PAGE), and Rf values of each of the protein band A, B, C and D on PAGE corresponded to that of bacteriolytic band a, b, c, and d, respectively, on PAGE containing cells of Micrococcus luteus reported previously (Takamoto et al., 1994). Finally, enzyme purified by cation-exchange chromatography contained a main protein band (B) and an indistinct protein band (E). The main protein band corresponded to bacteriolytic band b and was estimated to have a molecular weight of 74 kDa. Optimum pH and temperature for the activity of partially purified enzyme were 8.0 and 40 degrees C, respectively. It was inactivated completely by heating at 70 degrees C for 10 min
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