scholarly journals Does Subunit Composition Influence the Intermolecular Crosslinking of Fish Collagen? A Study with Hake and Blue Shark Skin Collagens

Polymers ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 1734 ◽  
Author(s):  
María Blanco ◽  
Noelia Sanz ◽  
Jesús Valcarcel ◽  
Ricardo I. Pérez-Martín ◽  
Carmen G. Sotelo
Keyword(s):  
Cation Exchange ◽  
Gel Permeation Chromatography ◽  
Exchange Chromatography ◽  
Subunit Composition ◽  
Chromatographic Behavior ◽  
Blue Shark ◽  
Shark Skin ◽  
Stirring Time ◽  
European Hake ◽  
Chromatographic Profiles

Acid-soluble collagens from European hake and Blue shark skin were isolated, characterized, and compared. As the structure of collagen determines its function, the final objective of this study was to investigate biochemical differences between both collagens to identify future potential applications. Chromatographic behavior revealed differences in collagen from both species. Increases of temperature and stirring time produced no effect on European hake collagen solubility in the mobile phase, resulting in the same chromatographic profiles. Conversely, the application of temperature and stirring-time increments showed a positive effect on Blue shark collagen solubility, resulting in different chromatographic profiles and observing higher molecular weight components when sample is incubated at 50 °C (15 min) after 48 h stirring. To test if the different chromatographic behavior exhibited by both collagens could be influenced by differences in subunit composition (alpha-chains), cation exchange chromatography was employed to separate collagen subunits. The electrophoretic patterns and gel permeation chromatography with light-scattering detection (GPC-LS) results of the obtained cation exchange peak fractions revealed differences regarding subunit composition between both species, influencing the crosslinking pattern. This is the first comparative study using GPC-LS to provide information of European hake and Blue shark collagen subunit composition.

Spray Drying of Blue Shark Skin Protein Hydrolysate: Physical, Morphological, and Antioxidant Properties

2014 ◽  
Vol 32 (16) ◽  
pp. 1986-1996 ◽  
Author(s):  
Julio C. Rodríguez-Díaz ◽  
Renata V. Tonon ◽  
Míriam D. Hubinger
Keyword(s):  
Spray Drying ◽  
Protein Hydrolysate ◽  
Antioxidant Properties ◽  
Blue Shark ◽  
Shark Skin ◽  
Skin Protein

scholarly journals The use of LC tandem mass spectrometry as part of a workflow for the screening and identification of hemoglobin variants. Characterization of Hb Ullevaal as an example

2017 ◽  
Vol 41 (3) ◽  
Author(s):  
Matthias Weber ◽  
Julia J.M. Eekels
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Cation Exchange ◽  
Peripheral Blood ◽  
Globin Gene ◽  
Reversed Phase ◽  
Exchange Chromatography ◽  
South Florida ◽  
Tandem Mass ◽  
Genetic Sequencing

AbstractBackground:About 2/3 of the hemoglobin (Hb) variants do not show a charge difference to the wildtype entity but most of them differ in hydrophobicity. In addition to cation exchange chromatography, globin differentiation by liquid chromatography-tandem mass spectrometry (MS) was introduced. Hb Ullevaal was chosen as one example to demonstrate the performance of the approach.Methods:Screening for Hb variants was performed using cation exchange HPLC. For globin separation reversed phase-LC/MS was performed. Tryptic digests of variants were separated on RP-HPLC with or without CID-fragmentation and database search for identification of mutation bearing fragments. Sequencing of the β-globin gene has been performed.Results:HbS, HbC, HbE, Hb South Florida and Hb Ullevaal show typical and distinct patterns in the globin LC/MS according to the theoretical protein data. The tryptic digest of Hb Ullevaal resulted in the identification of the respective mutated peptide βT9, which was confirmed by genetic sequencing.Conclusions:By the application of globin-LC/MS two more dimensions for the Hb identification are added, hydropathicity and protein mass. With this workflow as screening procedure for Hb variants it is expected to be able to detect and identify the majority of variants with the exception of highly unstable variants, which cannot be determined in the peripheral blood at all. A negative result makes the presence of a significant Hb variant in the peripheral blood improbable.

Strong cation-exchange chromatography of proteins on a sulfoalkylated monolithic cryogel

2015 ◽  
Vol 1386 ◽  
pp. 13-21 ◽  
Author(s):  
Işık Perçin ◽  
Rushd Khalaf ◽  
Bastian Brand ◽  
Massimo Morbidelli ◽  
Orhan Gezici
Keyword(s):  
Cation Exchange ◽  
Exchange Chromatography ◽  
Cation Exchange Chromatography ◽  
Strong Cation Exchange ◽  
Strong Cation Exchange Chromatography

scholarly journals Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus

1995 ◽  
Vol 308 (1) ◽  
pp. 243-249 ◽  
Author(s):  
J M C Ribeiro ◽  
M Schneider ◽  
J A Guimarães
Keyword(s):  
Cation Exchange ◽  
Salivary Glands ◽  
Coagulation Factor ◽  
Rhodnius Prolixus ◽  
Exchange Chromatography ◽  
Factor X ◽  
Blood Sucking ◽  
Weak Cation Exchange ◽  
Haem Protein ◽  
Strong Cation Exchange Chromatography

The salivary anticoagulant of the blood-sucking bug Rhodnius prolixus was purified to homogeneity using a protocol consisting of weak cation-exchange, DEAE, hydrophobic-interaction and octadecyl reverse-phase chromatography, yielding a protein with the same N-terminal sequence as nitrophorin 2, one of the four NO haem protein carriers present in the salivary glands of Rhodnius with a molecular mass of 19689 Da [D. Champagne, R.H. Nussenzveig and J.M.C. Ribeiro, (1995) J. Biol. Chem. 270, in the press]. To exclude the possibility of the nitrophorin being a contaminant, another chromatographic protocol was performed, consisting of chromatofocusing followed by strong-cation-exchange chromatography. Again the anticoagulant was eluted with nitrophorin 2. Nitrophorin 2 inhibits coagulation Factor VIII-mediated activation of Factor X and accounts for all the anti-clotting activity observed in Rhodnius salivary glands.

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