Isolation of a new toxic protease from a strain of Aeromonas salmonicida subspecies achromogenes.
BK Gudmundsdóttir, TS Hastings, AE Ellis - 1990 - cabidigitallibrary.org
BK Gudmundsdóttir, TS Hastings, AE Ellis
1990•cabidigitallibrary.orgA new toxic protease was isolated from A. salmonicida subspecies achromogenes
extracellular products (ECP). It was detected in 5 of 9 strains of the organism tested. The
protease was purified by anion-exchange fast protein liquid chromatography (FPLC) on
Mono Q HR 5/5, and FPLC gel filtration on Superose 12 HR 10/30. The LD50 of the purified
protease for juvenile Atlantic salmon (Salmo salar), was 0.03 µg protein/g fish. The
molecular weight of the protease was estimated to be 20 kD by SDS-polyacrylamide gel …
extracellular products (ECP). It was detected in 5 of 9 strains of the organism tested. The
protease was purified by anion-exchange fast protein liquid chromatography (FPLC) on
Mono Q HR 5/5, and FPLC gel filtration on Superose 12 HR 10/30. The LD50 of the purified
protease for juvenile Atlantic salmon (Salmo salar), was 0.03 µg protein/g fish. The
molecular weight of the protease was estimated to be 20 kD by SDS-polyacrylamide gel …
Abstract
A new toxic protease was isolated from A. salmonicida subspecies achromogenes extracellular products (ECP). It was detected in 5 of 9 strains of the organism tested. The protease was purified by anion-exchange fast protein liquid chromatography (FPLC) on Mono Q HR 5/5, and FPLC gel filtration on Superose 12 HR 10/30. The LD50 of the purified protease for juvenile Atlantic salmon (Salmo salar), was 0.03 µg protein/g fish. The molecular weight of the protease was estimated to be 20 kD by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and it possessed 2 isoelectric points (pIs) of 6.2 and 6.4. The protease was completely inhibited by EDTA indicating it to be a metallo-protease.
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