Characterization of the cathepsin B-like proteinases of Trichomonas tenax ATCC 30207.
An oral parasite Trichomonas tenax ATCC 30207 synthesizes and secretes various proteinases. By gelatin-SDS-PAGE, we found five proteinases bands (30, 37, 46, 51 and 60 kDa) in cell lysate and four bands (37, 45, 52 and 60 kDa) in culture filtrate. The proteinases hydrolyzed acid soluble type I collagen as well as gelatin. The enzymes were suggested to possess typical characteristics of cysteine proteinases based on the patterns of inhibition and activation by various factors. Based on relative efficiencies of synthetic substrates, most of them were most likely cathepsin B-like enzymes.
Yamamoto
A
A
Department of Oral Microbiology, Showa University, School of Dentistry, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
Asaga
E
E
Nagao
E
E
Igarashi
T
T
Goto
N
N
D000818:Animals; D002401:Cathepsin B / Q000737:chemistry* / Q000378:metabolism; D003094:Collagen / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D005780:Gelatin / Q000378:metabolism; D006868:Hydrolysis; D009055:Mouth / Q000469:parasitology; D011480:Protease Inhibitors / Q000378:metabolism; D015800:Protozoan Proteins / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity; D014244:Trichomonas / Q000201:enzymology*
D011480:Protease Inhibitors; D015800:Protozoan Proteins; D005780:Gelatin; D003094:Collagen; D002401:Cathepsin B