Interaction between cortisol and microbial proteases.
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.
Kuo
W N
WN
Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida.
Ganesan
U
U
Jean
M N
MN
Richardson
T B
TB
Robinson
A
A
Williams
A
A
Stone
N
N
Young
M
M
Noone
J
J
Burch
E J
EJ
D001419:Bacteria / Q000201:enzymology*; D010450:Endopeptidases / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005658:Fungi / Q000201:enzymology*; D006854:Hydrocortisone / Q000378:metabolism*; D066298:In Vitro Techniques
D004791:Enzyme Inhibitors; D010450:Endopeptidases; D006854:Hydrocortisone