Purification and characterization of a novel metalloprotease isolated from Aeromonas caviae.
A novel protease produced by Aeromonas caviae was purified and characterized. The molecular weight of the protease (AP19) was estimated as 19 kDa on SDS-polyacrylamide gel electrophoresis. The protease activity was not inhibited completely by heating at 100 degrees C for 15 min. The proteolytic activities were inhibited by metalloprotease inhibitor. The N-terminal amino acid sequence of AP19 was VTASVSFSGRCTN. AP19 did not activate Aeromonas proaerolysin, and did not show fluid accumulation in the rabbit intestinal loop test. A high concentration of the protease showed cytotoxic activity against Vero cells.
Division of Bacterial Pathogenesis, Department of Microbiology, Graduate School of Medicine, University of the Ryukyus, 207 Uehara, Okinawa 903-0215, Japan. noboru@med.u-ryukyu.ac.jp
Noboru
N
Nakasone
Claudia
C
Toma
Tianyan
T
Song
Masaaki
M
Iwanaga
D000333:Aeromonas / Q000201:enzymology*; D000818:Animals; D001427:Bacterial Toxins / Q000378:metabolism; D002522:Chlorocebus aethiops; D004591:Electrophoresis, Polyacrylamide Gel; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D006358:Hot Temperature; D007421:Intestine, Small / Q000382:microbiology / Q000473:pathology; D045726:Metalloproteases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D008970:Molecular Weight; D052899:Pore Forming Cytotoxic Proteins; D011817:Rabbits; D020539:Sequence Analysis, Protein; D014709:Vero Cells
D001427:Bacterial Toxins; D004791:Enzyme Inhibitors; D052899:Pore Forming Cytotoxic Proteins; C107096:proaerolysin; D045726:Metalloproteases