scholarly journals Multifunctional Cationic PeptoStars as siRNA Carrier: Influence of Architecture and Histidine Modification on Knockdown Potential

2019 ◽  
Vol 20 (1) ◽  
pp. 1900152 ◽  
Author(s):  
Regina Holm ◽  
David Schwiertz ◽  
Benjamin Weber ◽  
Jennifer Schultze ◽  
Jasmin Kuhn ◽  
...  
Keyword(s):  
Histidine Modification

Effect of histidine modification on the aging of organophosphate-inhibited acetylcholinesterase

1981 ◽  
Vol 30 (21) ◽  
pp. 2915-2920 ◽  
Author(s):  
Guy Beauregard ◽  
Joseph Lum ◽  
Basil D. Roufogalis
Keyword(s):  
Histidine Modification

Optimization of Fe3O4 nanozyme activity via single amino acid modification mimicking an enzyme active site

2017 ◽  
Vol 53 (2) ◽  
pp. 424-427 ◽  
Author(s):  
Kelong Fan ◽  
Hui Wang ◽  
Juqun Xi ◽  
Qi Liu ◽  
Xiangqin Meng ◽  
...  
Keyword(s):  
Amino Acid ◽  
Active Site ◽  
Catalytic Efficiency ◽  
Single Amino Acid ◽  
Acid Modification ◽  
Histidine Modification ◽  
Enzyme Active Site ◽  
Amino Acid Modification

Histidine modification effectively improved the affinity of Fe3O4 nanozyme to H2O2, enhancing its catalytic efficiency by mimicking peroxidase active site.

scholarly journals Effects of Histidine Modification on Kappa-casein

1973 ◽  
Vol 56 (6) ◽  
pp. 690-698 ◽  
Author(s):  
S. Nakai ◽  
W.G. Styles ◽  
J.J. Perrin
Keyword(s):  
Histidine Modification

Rh antigen immunoreactivity after histidine modification

1986 ◽  
Vol 23 (10) ◽  
pp. 1039-1044 ◽  
Author(s):  
Edward J. Victoria ◽  
Michael J. Branks ◽  
S.P. Masouredis
Keyword(s):  
Histidine Modification

Effects of histidine modification of chitosan microparticles on metal ion adsorption

2020 ◽  
Vol 154 ◽  
pp. 104694
Author(s):  
Marcella T. Maia ◽  
Débora N. Sena ◽  
Guilherme B. Calais ◽  
Francisco Murilo T. Luna ◽  
Marisa M. Beppu ◽  
...  
Keyword(s):  
Metal Ion ◽  
Ion Adsorption ◽  
Histidine Modification ◽  
Chitosan Microparticles ◽  
Metal Ion Adsorption

Inhibition of E. coli ʟ-Asparaginase by Reaction with 2,3-Butanedione. Chemical Modification of Arginine and Histidine Residues

1979 ◽  
Vol 34 (9-10) ◽  
pp. 742-746 ◽  
Author(s):  
Dorothee Petz ◽  
Hans-Gerhard Löffler ◽  
Friedh. Schneider
Keyword(s):  
Chemical Modification ◽  
Histidine Modification ◽  
Histidine Residues ◽  
E Coli ◽  
First Order ◽  
Complete Inactivation ◽  
First Order Kinetics ◽  
Competitive Inhibitors ◽  
Pseudo First Order

Abstract The inactivation of E. coli asparaginase by 2,3-butanedione studied with ʟ-asparagine and diazooxonorvaline as substrates obeys pseudo first order kinetics. Activity losses are linear with respect to arginine and histidine modification, with complete inactivation being correlated with alteration of one arginine and one histidine per subunit. The rate of inactivation of the enzym was reduced in the presence of competitive inhibitors like ʟ-2-amino-2-carboxyethane-sulfonamide. Un der comparable conditions 1,2-cyclo hexanedione does not affect the activity of ʟ-asparaginase.

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