"P(GP525/07/P253), P(OC09034), Z(MZE0002700604)" . . . . . . "Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites" . "251312" . "0739-4462" . "protease; digestion; enzyme; allergen; synanthropic acaridid mite"@en . "2"^^ . "20"^^ . "Erban, Tom\u00E1\u0161" . "3" . . . "Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites"@en . . "RIV/00027006:_____/10:00001292" . . . "Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites" . . "2"^^ . . "Archives of Insect Biochemistry and Physiology" . . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . . "Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites"@en . . "Microplate assays with 96 wells were optimized to screen proteolytic activities in mite homogenates. Whole-mite extracts of seven species of mites exhibited non-specific proteolytic activity in buffers from pH 2 to 12, and three peaks of highest activity at pH 3, 5-6, and 10 were distinguished. The reducing agent Tris(2-carboxyethyl) phosphine hydrochloride decreased general proteolytic activity on azocasein at pH 5 and 6. The results obtained on two non-specific substrates, azocasein and azoalbumin, showed highly different ranks of the species at pH 5 and 6. Evidence of the presence of proteolytic activities on all tested substrates and in all the tested mite homogenates suggests that the proteolytic activities may contribute to allergenicity. Poor or undetected hydrolytic activities of mite extracts toward substrates for keratin and collagen at digestive pH underline the importance of ecological interactions between mites and microorganisms in the utilization of such substrates."@en . "Hubert, Jan" . "[E99DB710EF00]" . "000283778200004" . . . . . . "Microplate assays with 96 wells were optimized to screen proteolytic activities in mite homogenates. Whole-mite extracts of seven species of mites exhibited non-specific proteolytic activity in buffers from pH 2 to 12, and three peaks of highest activity at pH 3, 5-6, and 10 were distinguished. The reducing agent Tris(2-carboxyethyl) phosphine hydrochloride decreased general proteolytic activity on azocasein at pH 5 and 6. The results obtained on two non-specific substrates, azocasein and azoalbumin, showed highly different ranks of the species at pH 5 and 6. Evidence of the presence of proteolytic activities on all tested substrates and in all the tested mite homogenates suggests that the proteolytic activities may contribute to allergenicity. Poor or undetected hydrolytic activities of mite extracts toward substrates for keratin and collagen at digestive pH underline the importance of ecological interactions between mites and microorganisms in the utilization of such substrates." . "RIV/00027006:_____/10:00001292!RIV11-GA0-00027006" . "75" . .