Macromolecular Crowding Effect on the Activity of Liposome-Bound Alkaline Phosphatase: A Paradoxical Inhibitory Action

Langmuir ◽  
2021 ◽  
Author(s):  
Akshi Deshwal ◽  
Subhabrata Maiti
Keyword(s):  
Alkaline Phosphatase ◽  
Inhibitory Action ◽  
Macromolecular Crowding ◽  
Crowding Effect

scholarly journals Amplifying the Macromolecular Crowding Effect Using Nanoparticles

2011 ◽  
Vol 134 (1) ◽  
pp. 35-38 ◽  
Author(s):  
Ahmed Zaki ◽  
Neeshma Dave ◽  
Juewen Liu
Keyword(s):  
Macromolecular Crowding ◽  
Crowding Effect

scholarly journals Oxidative folding of hirudin in human serum

2006 ◽  
Vol 394 (1) ◽  
pp. 249-257 ◽  
Author(s):  
Jui-Yoa Chang ◽  
Bao-Yun Lu ◽  
Por-Hsiung Lai
Keyword(s):  
Amino Acids ◽  
Protein Folding ◽  
Human Serum ◽  
Initial Phase ◽  
Macromolecular Crowding ◽  
Specific Inhibitor ◽  
Crowding Effect ◽  
Oxidative Folding ◽  
Disulphide Bonds ◽  
Kinetics Of

Human serum contains factors that promote oxidative folding of disulphide proteins. We demonstrate this here using hirudin as a model. Hirudin is a leech-derived thrombin-specific inhibitor containing 65 amino acids and three disulphide bonds. Oxidative folding of hirudin in human serum is shown to involve an initial phase of rapid disulphide formation (oxidation) to form the scrambled isomers as intermediates. This is followed by the stage of slow disulphide shuffling of scrambled isomers to attain the native hirudin. The kinetics of regenerating the native hirudin depend on the concentrations of both hirudin and human serum. Quantitative regeneration of native hirudin in undiluted human serum can be completed within 48 h, without any redox supplement. These results cannot be adequately explained by the existing oxidized thiol agents in human serum or the macromolecular crowding effect, and therefore indicate that human serum may contain yet to be identified potent oxidase(s) for assisting protein folding.

Macromolecular crowding effect for photoreactions of LOV2 domains of Arabidopsis thaliana phototropin 1

2016 ◽  
Vol 217 ◽  
pp. 43-50
Author(s):  
Tomoyuki Yoshitake ◽  
Tsuguyoshi Toyooka ◽  
Yusuke Nakasone ◽  
Kazunori Zikihara ◽  
Satoru Tokutomi ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Macromolecular Crowding ◽  
Crowding Effect

scholarly journals Macromolecular Crowding Effect uponin VitroEnzyme Kinetics: Mixed Activation–Diffusion Control of the Oxidation of NADH by Pyruvate Catalyzed by Lactate Dehydrogenase

2014 ◽  
Vol 118 (15) ◽  
pp. 4062-4068 ◽  
Author(s):  
Cristina Balcells ◽  
Isabel Pastor ◽  
Eudald Vilaseca ◽  
Sergio Madurga ◽  
Marta Cascante ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Macromolecular Crowding ◽  
Diffusion Control ◽  
Crowding Effect

Difference in Binding of Long- and Medium-Chain Fatty Acids with Serum Albumin: The Role of Macromolecular Crowding Effect

2018 ◽  
Vol 66 (5) ◽  
pp. 1242-1250 ◽  
Author(s):  
Tian-Tian Zhu ◽  
Yan Zhang ◽  
Xing-An Luo ◽  
Shen-Zhi Wang ◽  
Ming-Qiang Jia ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Serum Albumin ◽  
Macromolecular Crowding ◽  
Crowding Effect ◽  
Medium Chain ◽  
Medium Chain Fatty Acids ◽  
Chain Fatty Acids

scholarly journals Localization of Protein Aggregation in Escherichia coli Is Governed by Diffusion and Nucleoid Macromolecular Crowding Effect

2013 ◽  
Vol 9 (4) ◽  
pp. e1003038 ◽  
Author(s):  
Anne-Sophie Coquel ◽  
Jean-Pascal Jacob ◽  
Mael Primet ◽  
Alice Demarez ◽  
Mariella Dimiccoli ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Aggregation ◽  
Macromolecular Crowding ◽  
Crowding Effect
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