Characterization of the proteases in the crude mite extract.
Characterization of the proteases was performed in the crude mite extract fractionated by Sephacryl S-200 gel filtration. Three peaks of protease activities were detected in the fractions. From the results of substrate specificity and susceptibility to the inhibitors, PK.1 protease (about 60 kD) is suggested to be a trypsin-like protease of mites. From the results of susceptibility to various agents, PK.2 (about 30 kD) and PK.3 (about 20 kD) proteases may be cysteine proteases, e.g., papain and cathepsin B. PK.3 protease existed in the precipitate of 60% ammonium sulfate fractionation. The data in the present study suggest the possibility that Dermatophagoides farinae I allergen might be a cysteine protease probably derived from the gastrointestinal tract of the house dust mite.
Ino
Y
Y
Research Laboratories, Torii & Co., Ltd., Ichikawa, Japan.
Ando
T
T
Haida
M
M
Nakamura
K
K
Iwaki
M
M
Okudaira
H
H
Miyamoto
T
T
D000485:Allergens; D000645:Ammonium Sulfate; D000818:Animals; D039741:Antigens, Dermatophagoides; D002474:Cell-Free System; D005591:Chemical Fractionation; D002850:Chromatography, Gel; D004391:Dust / Q000032:analysis; D004789:Enzyme Activation; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008925:Mites / Q000201:enzymology* / Q000276:immunology; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology
D000485:Allergens; D039741:Antigens, Dermatophagoides; D004391:Dust; D011480:Protease Inhibitors; D010447:Peptide Hydrolases; D000645:Ammonium Sulfate