RESUMO
Human saliva was tested for the presence of factors that affect the complement system. Parotid saliva and salivary fractions were incubated at 37 C with human serum as a source of complement. Samples removed from the mixtures within the first 15 minutes had higher levels of whole hemolytic complement activity than did appropriate controls. The final ionic strength of the saliva-serum mixtures was critical to the hemolytic activity of complement. After 60 minutes all serum-saliva mixtures had lower levels of hemolytic activity than did serum-buffer controls. With regard to whole saliva, the salivary sediment was found to be strongly complement-reactive.
Assuntos
Proteínas do Sistema Complemento/fisiologia , Hemólise , Saliva/fisiologia , Animais , Soluções Tampão , Eritrócitos/imunologia , Eritrócitos/fisiologia , Humanos , Glândula Parótida , Ovinos , Cloreto de Sódio/farmacologiaRESUMO
Thermomonospora curvata produces an extracellular alpha-amylase. Maximal amylase production by cultures in a starch-mineral salts medium occurred at pH 7.5 and 53 degrees C. The crude enzyme was unstable to heating (65 degrees C) at pH 4 to 6, and was activated when heated at pH 8. The enzyme was purified 66-fold with a 9% yield and appeared homogeneous on discontinuous gel electrophoresis. The pH and temperature optima for activity of the purified enzyme were 5.5 to 6.0 and 65 degrees C. The molecular weight was calculated to be 62,000. The Km for starch was 0.39 mg/ml. The amylolytic pattern consisted of a mixture of maltotetraose and maltopentaose.