Autor: |
W N, Kuo, U, Ganesan, M N, Jean, T B, Richardson, A, Robinson, A, Williams, N, Stone, M, Young, J, Noone, E J, Burch |
Rok vydání: |
1989 |
Předmět: |
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Zdroj: |
Cytobios. 59(238-239) |
ISSN: |
0011-4529 |
Popis: |
Binding (or interaction) of cortisol with microbial molecule(s) was observed by employing Bio-Gel HTP affinity chromatography and subsequently by fluorescence spectrophotometry. Molecule(s) in the crude extract of baker's yeast and in other microbial proteases exhibited varied degrees of cortisol-binding. Bacterial protease (type IX) had highest, while the type XXVI enzyme had the lowest, binding capacity. In addition, these two proteases exhibited a distinct difference in the alterations of ultraviolet spectra due to interaction with cortisol. Using casein as a substrate, cortisol, CTP, trypsin inhibitor or leupeptin appreciably inhibited type IX protease at low concentrations of Ca2+. However, thyroxine had no effect on this protease. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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