muramidase and drospirenone

muramidase has been researched along with drospirenone* in 1 studies

Other Studies

1 other study(ies) available for muramidase and drospirenone

Article	Year
Binding properties of drospirenone with human serum albumin and lysozyme in vitro. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2016, Jan-15, Volume: 153 The interaction of drospirenone (DP) with human serum albumin (HSA)/lysozyme (LYZ) was investigated using different optical techniques and molecular models. Results from the emission and time resolved fluorescence studies revealed that HSA/LYZ emission quenching with DP was initiated by static quenching mechanism. The LYZ-DP system was more easily influenced by temperature than the HSA-DP system. Displacement experiments demonstrated that the DP binding site was mainly located in site 1 of HSA. Based on the docking methods, DP was mainly bound in the active site hinge region where Trp-62 and Trp-63 are located. Conformation study showed that DP had different effects on the local conformation of HSA and LYZ molecules. Topics: Androstenes; Animals; Catalytic Domain; Chickens; Circular Dichroism; Humans; Kinetics; Models, Molecular; Muramidase; Protein Binding; Serum Albumin; Spectrometry, Fluorescence; Temperature; Time Factors	2016

Article

Year

Binding properties of drospirenone with human serum albumin and lysozyme in vitro.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 2016, Jan-15, Volume: 153

The interaction of drospirenone (DP) with human serum albumin (HSA)/lysozyme (LYZ) was investigated using different optical techniques and molecular models. Results from the emission and time resolved fluorescence studies revealed that HSA/LYZ emission quenching with DP was initiated by static quenching mechanism. The LYZ-DP system was more easily influenced by temperature than the HSA-DP system. Displacement experiments demonstrated that the DP binding site was mainly located in site 1 of HSA. Based on the docking methods, DP was mainly bound in the active site hinge region where Trp-62 and Trp-63 are located. Conformation study showed that DP had different effects on the local conformation of HSA and LYZ molecules.

Topics: Androstenes; Animals; Catalytic Domain; Chickens; Circular Dichroism; Humans; Kinetics; Models, Molecular; Muramidase; Protein Binding; Serum Albumin; Spectrometry, Fluorescence; Temperature; Time Factors

2016