Displacement Chromatography in the Separation and Characterization of Proteins and Peptides

2010 ◽  
pp. 309-327 ◽  
Author(s):  
James Wilkins
Keyword(s):  
Displacement Chromatography ◽  
Proteins And Peptides

Characterization of Venoms of Deinagkistrodon acutus and Bungarus multicinctus Using Proteomics and Peptidomics

2020 ◽  
Vol 17 (3) ◽  
pp. 241-254
Author(s):  
Yaqiong Zhang ◽  
Zhiping Jia ◽  
Yunyang Liu ◽  
Xinwen Zhou ◽  
Yi Kong
Keyword(s):  
Snake Venom ◽  
Protein Families ◽  
Traditional Medicines ◽  
Phospholipases A2 ◽  
Inhibitory Peptides ◽  
Sds Page ◽  
Deinagkistrodon Acutus ◽  
Venom Proteins ◽  
Proteins And Peptides

Background: Deinagkistrodon acutus (D. acutus) and Bungarus multicinctus (B. multicinctus) as traditional medicines have been used for hundreds of years in China. The venoms of these two species have strong toxicity on the victims. Objective: The objective of this study is to reveal the profile of venom proteins and peptides of D. acutus and B. multicinctus. Method: Ultrafiltration, SDS-PAGE coupled with in-gel tryptic digestion and Liquid Chromatography- Electrospray Ionization-Tandem Mass Spectrometry (LC-ESI-MS/MS) were used to characterize proteins and peptides of venoms of D. acutus and B. multicinctus. Results: In the D. acutus venom, 67 proteins (16 protein families) were identified, and snake venom metalloproteinases (SVMPs, 38.0%) and snake venom C-type lectins (snaclecs, 36.7%) were dominated proteins. In the B. multicinctus venom, 47 proteins (15 protein families) were identified, and three-finger toxins (3FTxs, 36.3%) and Kunitz-type Serine Protease Inhibitors (KSPIs, 32.8%) were major components. In addition, both venoms contained small amounts of other proteins, such as Snake Venom Serine Proteinases (SVSPs), Phospholipases A2 (PLA2s), Cysteine-Rich Secreted Proteins (CRISPs), 5'nucleotidases (5'NUCs), Phospholipases B (PLBs), Phosphodiesterases (PDEs), Phospholipase A2 Inhibitors (PLIs), Dipeptidyl Peptidases IV (DPP IVs), L-amino Acid Oxidases (LAAOs) and Angiotensin-Converting Enzymes (ACEs). Each venom also had its unique proteins, Nerve Growth Factors (NGFs) and Hyaluronidases (HYs) in D. acutus, and Cobra Venom Factors (CVFs) in B. multicinctus. In the peptidomics, 1543 and 250 peptides were identified in the venoms of D. acutus and B. multicinctus, respectively. Some peptides showed high similarity with neuropeptides, ACE inhibitory peptides, Bradykinin- Potentiating Peptides (BPPs), LAAOs and movement related peptides. Conclusion: Characterization of venom proteins and peptides of D. acutus and B. multicinctus will be helpful for the treatment of envenomation and drug discovery.

scholarly journals Proteomic Advances in Milk and Dairy Products

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 3832
Author(s):  
Rubén Agregán ◽  
Noemí Echegaray ◽  
María López-Pedrouso ◽  
Radwan Kharabsheh ◽  
Daniel Franco ◽  
...  
Keyword(s):  
Dairy Products ◽  
Two Dimensional Gel Electrophoresis ◽  
Vast Number ◽  
Post Translational Modifications ◽  
Fundamental Parameters ◽  
Complex Fluid ◽  
Proteins And Peptides ◽  
Milk And Dairy Products

Proteomics is a new area of study that in recent decades has provided great advances in the field of medicine. However, its enormous potential for the study of proteomes makes it also applicable to other areas of science. Milk is a highly heterogeneous and complex fluid, where there are numerous genetic variants and isoforms with post-translational modifications (PTMs). Due to the vast number of proteins and peptides existing in its matrix, proteomics is presented as a powerful tool for the characterization of milk samples and their products. The technology developed to date for the separation and characterization of the milk proteome, such as two-dimensional gel electrophoresis (2DE) technology and especially mass spectrometry (MS) have allowed an exhaustive characterization of the proteins and peptides present in milk and dairy products with enormous applications in the industry for the control of fundamental parameters, such as microbiological safety, the guarantee of authenticity, or the control of the transformations carried out, aimed to increase the quality of the final product.

Characterization of proteins separated by displacement chromatography using low angle laser light scattering photometry

1994 ◽  
Vol 38 (5-6) ◽  
pp. 349-354 ◽  
Author(s):  
R. Mhatre ◽  
R. Qian ◽  
I. S. Krull ◽  
S. Gadam ◽  
S. M. Cramer
Keyword(s):  
Light Scattering ◽  
Laser Light ◽  
Laser Light Scattering ◽  
Displacement Chromatography

Disulfide Linkage Characterization of Disulfide Bond-Containing Proteins and Peptides by Reducing Electrochemistry and Mass Spectrometry

2016 ◽  
Vol 88 (3) ◽  
pp. 1585-1592 ◽  
Author(s):  
Christian N. Cramer ◽  
Kim F. Haselmann ◽  
Jesper V. Olsen ◽  
Peter Kresten Nielsen
Keyword(s):  
Mass Spectrometry ◽  
Disulfide Bond ◽  
Disulfide Linkage ◽  
Proteins And Peptides

scholarly journals Environment-Sensitive Fluorescent Labelling of Peptides by Luciferin Analogues

2021 ◽  
Vol 22 (24) ◽  
pp. 13312
Author(s):  
Marialuisa Siepi ◽  
Rosario Oliva ◽  
Antonio Masino ◽  
Rosa Gaglione ◽  
Angela Arciello ◽  
...  
Keyword(s):  
Laser Scanning ◽  
Emission Spectra ◽  
Water Concentration ◽  
Solvent Polarity ◽  
Firefly Luciferase ◽  
Laser Scanning Microscopy ◽  
Confocal Laser ◽  
Water Abundance ◽  
Proteins And Peptides

Environment-sensitive fluorophores are very valuable tools in the study of molecular and cellular processes. When used to label proteins and peptides, they allow for the monitoring of even small variations in the local microenvironment, thus acting as reporters of conformational variations and binding events. Luciferin and aminoluciferin, well known substrates of firefly luciferase, are environment-sensitive fluorophores with unusual and still-unexploited properties. Both fluorophores show strong solvatochromism. Moreover, luciferin fluorescence is influenced by pH and water abundance. These features allow to detect local variations of pH, solvent polarity and local water concentration, even when they occur simultaneously, by analyzing excitation and emission spectra. Here, we describe the characterization of (amino)luciferin-labeled derivatives of four bioactive peptides: the antimicrobial peptides GKY20 and ApoBL, the antitumor peptide p53pAnt and the integrin-binding peptide RGD. The two probes allowed for the study of the interaction of the peptides with model membranes, SDS micelles, lipopolysaccharide micelles and Escherichia coli cells. Kd values and binding stoichiometries for lipopolysaccharide were also determined. Aminoluciferin also proved to be very well-suited to confocal laser scanning microscopy. Overall, the characterization of the labeled peptides demonstrates that luciferin and aminoluciferin are previously neglected environment-sensitive labels with widespread potential applications in the study of proteins and peptides.

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