Identification, purification, biochemical and mass spectrometric characterization of novel phycobiliproteins from a marine red alga, Centroceras clavulatum

Nair, Divya; Krishna, Jissa Gopala; Panikkar, M. V. N.; Nair, Bipin G.; Pai, Jayashree Gopalakrishna; Nair, Sudarslal Sadasivan

doi:10.1016/j.ijbiomac.2018.03.153

Cited by 27 publications

(17 citation statements)

References 47 publications

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“…For the protein identification we used a nano flow HPLC (Agilent 1260 series) coupled to a Q‐TOF mass spectrometer (6540 series, Agilent Technologies, USA) equipped with a Chip‐Cube interface. The chymotrypsin digested samples were infused through a Zorbax SB‐C 18 reversed‐phase chip containing an enrichment column and a separation column (Nair et al, 2018). The mobile phases A and B were water and 90% acetonitrile both containing 0.1% formic acid.…”

Section: Methodsmentioning

confidence: 99%

Identification of carbonylated proteins from monocytic cells under diabetes‐induced stress conditions

Nair

Nedungadi

Mishra

et al. 2021

Biomedical Chromatography

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Diabetes is a metabolic disorder characterized by the presence of elevated glucose in the blood and enhanced oxidative stress. It affects the cellular homeostasis that leads to the development of micro‐and macro‐vascular complications. Monocytes are the primary immune cells present in the circulatory system. Under high‐glucose conditions, the cells undergo oxidative stress and secrete reactive oxygen species. The enhanced release of reactive species is known to modify biomolecules like proteins and nucleic acids. Protein carbonylation, one of the most harmful and irreversible protein modifications, is considered as a key player in the progression of diabetes and associated complications. Hence, the present study explores the identification of carbonylated proteins from the monocytes under diabetic stress and determination of their site of modification. Combined avidin affinity chromatography and bottom‐up proteomics experiments identified 13 consistently expressed carbonylated proteins. Most of the identified proteins were reported to have altered functions under diabetic conditions that contribute to the development of diabetes‐associated inflammation and complications. We were able to determine oxidative stress‐induced modifications on Lys, Val, Ile, Cys, Thr and Asp residues.

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Section: Methodsmentioning

confidence: 99%

Identification of carbonylated proteins from monocytic cells under diabetes‐induced stress conditions

Nair

Nedungadi

Mishra

et al. 2021

Biomedical Chromatography

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“…PBPs are brightly colored, highly fluorescent, water-soluble, covalently attached linear tetrapyrolic pigments that are structurally related to the bile pigment biliverdin and have a spectrum of applications (Nair et al, 2018). These protein compounds constitute important components of lightharvesting complexes of the photosynthetic machinery in cyanobacteria (blue-green algae), red algae, and cryptomonads (Manirafasha et al, 2016).…”

Section: Phycobiliproteinsmentioning

confidence: 99%

“…PBPs have been isolated as distinct subunits as either trimers (αβ) 3 , of approximately M r 110-120 kDa (e.g., allophycocyanins) or hexamers (αβ) 6γ of about M r 250 kDa (certain phycoerythrins) (Glazer, 1994). PBPs are conveniently classified according to their spectral properties and these spectroscopic properties of PBPs are determined by the presence of different chromophores known as phycobilins (Nair et al, 2018). Phycoerythrins are most abundant in red algae and some unicellular cyanobacteria.…”

Section: Phycobiliproteinsmentioning

confidence: 99%

“…Besides spectral properties, PBPs are classified into two large groups based on their brilliant colors, the phycoerythrin (red), and the phycocyanin (blue). Due to their distinct physicochemical properties, PBS are also classified into phycoerythrocyanin, R-phycoerythrin, B-phycoerythrin, phycocyanin, and allophycocyanin which have important applications as fluorescent tags in flow cytometry, fluorescence-activated cell sorting, histochemistry, immunoassay and detection of reactive oxygen species (Nair et al, 2018). Besides, PBPs have major applications in natural dyes in the food industry and pharmaceutical products.…”

Section: Phycobiliproteinsmentioning

confidence: 99%

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Biotechnological Applications of Microalgal Oleaginous Compounds: Current Trends on Microalgal Bioprocessing of Products

et al. 2020

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The microalgal biotechnology industry is expanding rapidly and currently gaining attention due to multiple availabilities of high-value products such as pigments, carbohydrates, proteins, nutraceuticals, biopharmaceuticals, and unique oleaginous compounds fractionated by biomass biorefinery. Microalgae are efficient primary producers in the terrestrial and marine biotopes. They are major sources of global oxygen and are gaining topical prominence due to their concomitant role in the phycoremediation of wastewater effluents and biomass production. Despite their minuscule size, microalgae critically contribute to climate change mitigation through carbon fixation and play a major role in bioenergy applications. Furthermore, carotenoids and phycobiliproteins are the main accessory light-harvesting complexes in microalgae and cyanobacteria. The topical biomedical and pharmaceutical applications of microalgae include anticancer, antidiabetic, antiHIV, antimalarial, antimicrobial, inter alia. The endowment of unique indigenous microalgae and utilization of these biological resources must be harnessed by the biorefinery industry to exploit microalgal biomass opportunities. Therefore, this manuscript factually and critically explores the current status of the biorefinery approach, topical biomedical and pharmaceutical applications, biofuel applications, genetic manipulation of microalgae for enhancement of product yield, challenges and presents prospects, pros and cons, and outlook of the microalgal biotechnology industry.

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“…Indeed, preliminary MS work has already been utilized to reveal details on the bilin architecture and amino acid sequence of the g subunit in R-phycoerythrin. 26,27 The combination of multiple MS approaches provides complementary information that is not obtainable from a single MS method, which proved to be advantageous for the analysis of highly heterogeneous proteins and protein complexes. 25,[28][29][30] Here, we use a combination of bottom-up, top-down, and native MS to explore the structural heterogeneity present within the protein assembly B-PE and its constituent subunits in the red algae P. cruentum.…”

Section: Introductionmentioning

confidence: 99%

A Colorful Pallet of B-Phycoerythrin Proteoforms Exposed by a Multimodal Mass Spectrometry Approach

Tamara

Hoek

Scheltema

et al. 2019

Chem

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B-phycoerythrin is an extremely heterogeneous protein assembly comprising 13 subunits, all decorated with numerous chromophores. By combining different tiers of mass spectrometric analysis, native MS, top-down MS, and bottom-up MS, Tamara et al. characterize B-phycoerythrin in great detail. Integrating the data allowed them to identify all co-occurring proteoforms within B-phycoerythrin and identify the chemical nature and exact localization of all chromophores they harbor. Knowledge of these structural heterogeneities will be beneficial for the future design of even more efficient light-harvesting systems.

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Identification, purification, biochemical and mass spectrometric characterization of novel phycobiliproteins from a marine red alga, Centroceras clavulatum

Cited by 27 publications

References 47 publications

Identification of carbonylated proteins from monocytic cells under diabetes‐induced stress conditions

Identification of carbonylated proteins from monocytic cells under diabetes‐induced stress conditions

Biotechnological Applications of Microalgal Oleaginous Compounds: Current Trends on Microalgal Bioprocessing of Products

A Colorful Pallet of B-Phycoerythrin Proteoforms Exposed by a Multimodal Mass Spectrometry Approach

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