Spontaneous inactivation of human lung tryptase as probed by size-exclusion chromatography and chemical cross-linking: dissociation of active tetrameric enzyme into inactive monomers is the primary event of the entire process

1998 ◽  
Vol 1385 (1) ◽  
pp. 139-148 ◽  
Author(s):  
Andrzej Kozik ◽  
Jan Potempa ◽  
James Travis
Keyword(s):  
Size Exclusion Chromatography ◽  
Human Lung ◽  
Size Exclusion ◽  
Cross Linking ◽  
Primary Event ◽  
Entire Process ◽  
Exclusion Chromatography ◽  
Chemical Cross Linking

scholarly journals Expanding the Chemical Cross-Linking Toolbox by the Use of Multiple Proteases and Enrichment by Size Exclusion Chromatography

2012 ◽  
Vol 11 (3) ◽  
pp. M111.014126 ◽  
Author(s):  
Alexander Leitner ◽  
Roland Reischl ◽  
Thomas Walzthoeni ◽  
Franz Herzog ◽  
Stefan Bohn ◽  
...  
Keyword(s):  
Size Exclusion Chromatography ◽  
Size Exclusion ◽  
Cross Linking ◽  
Exclusion Chromatography ◽  
Chemical Cross Linking

scholarly journals Size Modulation of Enzymatically Cross-Linked Sodium Caseinate Nanoparticles via Ionic Strength Variation Affects the Properties of Acid-Induced Gels

Dairy ◽  
2021 ◽  
Vol 2 (1) ◽  
pp. 148-164
Author(s):  
Norbert Raak ◽  
Lars Leonhardt ◽  
Harald Rohm ◽  
Doris Jaros
Keyword(s):  
Molecular Structure ◽  
Ionic Strength ◽  
Structure Function ◽  
Size Exclusion Chromatography ◽  
Functional Properties ◽  
Sodium Caseinate ◽  
Size Exclusion ◽  
Cross Linking ◽  
Food Proteins ◽  
Exclusion Chromatography

Enzymatic cross-linking by microbial transglutaminase is a prominent approach to modify the structure and techno-functional properties of food proteins such as casein. However, some of the factors that influence structure-function-interrelations are still unknown. In this study, the size of cross-linked sodium caseinate nanoparticles was modulated by varying the ionic milieu during incubation with the enzyme. As was revealed by size exclusion chromatography, cross-linking at higher ionic strength resulted in larger casein particles. These formed acid-induced gels with higher stiffness and lower susceptibility to forced syneresis compared to those where the same number of ions was added after the cross-linking process. The results show that variations of the ionic milieu during enzymatic cross-linking of casein can be helpful to obtain specific modifications of its molecular structure and certain techno-functional properties. Such knowledge is crucial for the design of protein ingredients with targeted structure and techno-functionality.

Autoxidative Degradation of Poly(phenylacetylene)

1993 ◽  
Vol 58 (11) ◽  
pp. 2651-2662 ◽  
Author(s):  
Jiří Vohlídal ◽  
Dana Rédrová ◽  
Marta Pacovská ◽  
Jan Sedláček
Keyword(s):  
Molecular Weight ◽  
Solid State ◽  
Induction Period ◽  
High Molecular Weight ◽  
Size Exclusion Chromatography ◽  
Main Chain ◽  
Size Exclusion ◽  
Cross Linking ◽  
Exclusion Chromatography ◽  
High Molecular Weight Poly

Autooxidative degradation of high molecular-weight poly(phenylacetylene) (PPhA) in solid state and in solution was studied using the size exclusion chromatography (SEC) and UV, IR, and EPR spectrometry. No degradation was observed on PPhA stored in vacuum, whereas the polymer exposed to air was found to degrade without any induction period. No evidence of a cross-linking of oxidized PPhA was observed. The degradation of PPhA was found to be: (i) practically non-influenced by an ambient, diffuse day-light; (ii) of the random type (i.e. each main-chain bond of PPhA has the same probability of being ruptured); and (iii) fast enough to influence the results of SEC measurements.

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