The benzene metabolite p-benzoquinone inhibits the catalytic activity of bovine liver catalase: A biophysical study

2020 ◽  
Author(s):  
Atala B. Jena ◽  
Rashmi R. Samal ◽  
Kanchan Kumari ◽  
Jyotsnarani Pradhan ◽  
Gagan B.N. Chainy ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Bovine Liver ◽  
Biophysical Study ◽  
Bovine Liver Catalase

scholarly journals Cationic gemini surfactant stimulates amyloid fibril formation in bovine liver catalase at physiological pH. A biophysical study

RSC Advances ◽  
2020 ◽  
Vol 10 (71) ◽  
pp. 43751-43761
Author(s):  
Javed Masood Khan ◽  
Ajamaluddin Malik ◽  
Md. Tabish Rehman ◽  
Mohamed F. AlAjmi ◽  
Mohammad Z. Ahmed ◽  
...  
Keyword(s):  
Gemini Surfactant ◽  
Amyloid Fibril ◽  
Bovine Liver ◽  
Fibril Formation ◽  
Conformational Switching ◽  
Cationic Gemini Surfactant ◽  
Amyloid Fibril Formation ◽  
Biophysical Study ◽  
Bovine Liver Catalase ◽  
Amyloid Fibrillation

Surfactant molecules stimulate amyloid fibrillation and conformational switching in proteins but the mechanisms by which they accomplish these effects are unclear.

The molecular symmetry of bovine liver catalase

1975 ◽  
Vol 93 (1) ◽  
pp. 55-62 ◽  
Author(s):  
William Eventoff ◽  
G.V. Gurskaya
Keyword(s):  
Bovine Liver ◽  
Molecular Symmetry ◽  
Bovine Liver Catalase

scholarly journals Half-sites oxidation of bovine liver uridine diphosphate glucose dehydrogenase

1978 ◽  
Vol 173 (2) ◽  
pp. 701-704 ◽  
Author(s):  
J S Franzen ◽  
P Marchetti ◽  
R Ishman ◽  
J Ashcom
Keyword(s):  
Catalytic Activity ◽  
Glucose Dehydrogenase ◽  
Bovine Liver ◽  
Thiol Group ◽  
Catalytic Site ◽  
Uridine Diphosphate ◽  
Thiol Groups ◽  
Irreversible Denaturation ◽  
Diphosphate Glucose ◽  
Uridine Diphosphate Glucose Dehydrogenase

6,6-Dithiodinicotinate shows half-of-the-sites reactivity towards the six catalytic-site thiol groups of bovine liver UDP-glucose dehydrogenase. The reagent introduces three intrasubunit disulphide linkages between catalytic-site thiol groups and non-catalytic-site thiol groups and abrogates 60% of the catalytic activity of the hexameric enzyme; excess 2-mercaptoethanol rapidly restores full catalytic activity. These results show the half-of-the-sites behaviour of the enzyme with the reagent and the presence of a non-catalytic-site thiol group capable of forming a disulphide linkage with a catalytic-site thiol group on the same subunit without irreversible denaturation.

Molecular docking and inhibitory effects of a novel cytotoxic agent with bovine liver catalase

2020 ◽  
Vol 1205 ◽  
pp. 127590
Author(s):  
Somaye Shahraki ◽  
Maryam Saeidifar ◽  
Hojat Samareh Delarami ◽  
Houman Kazemzadeh
Keyword(s):  
Molecular Docking ◽  
Bovine Liver ◽  
Cytotoxic Agent ◽  
Inhibitory Effects ◽  
Bovine Liver Catalase
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