The primary structure of a novel riboflavin-binding protein of emu (Dromaius novaehollandiae)

Maehashi, Kenji; Matano, Mami; Uchino, Makoto; Yamämoto, Yasushi; Tanaka, Katsumi

doi:10.1016/j.cbpb.2009.02.004

Cited by 6 publications

(6 citation statements)

References 27 publications

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“…We reported in our previous study that emu egg albumen contained a riboflavinbinding protein of 50 kDa, which showed a 30 kDa band after deglycosylation. 23 A 50 kDa protein, reduced in size after deglycosylation, of the ppt fraction was identified as TENP by protein sequencing and we thereby concluded that emu TENP is an N-glycosylated protein as predicted from its amino acid sequence. The deglycosylation also confirmed that the ppt fraction was not contaminated with RBP.…”

Section: ■ Results and Discussionmentioning

confidence: 68%

Biochemical and Functional Characterization of Transiently Expressed in Neural Precursor (TENP) Protein in Emu Egg White

Maehashi

Ueda

Matano

et al. 2014

J. Agric. Food Chem.

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A protein transiently expressed in the neural precursors of developing tissues (TENP) was found to be present in emu (Dromaius novaehollandiae) egg white as one of the major proteins. Nucleotide analysis of its encoding cDNA revealed a sequence of 452 amino acids including a 19 amino acid peptide signal. Phylogenetic analysis determined that emu TENP was clustered within the bactericidal/permeability-increasing protein (BPI) superfamily together with other avian TENPs. RT-PCR analysis revealed that the emu TENP gene was highly expressed in the magnum of the oviduct, indicating that TENP is a major egg white component. Emu TENP was purified by anion exchange chromatography and ammonium sulfate fractionation. Unlike BPI, emu TENP exhibited antibacterial activity against Gram-positive bacteria, including Micrococcus luteus and Bacillus subtilis, but not against Gram-negative bacteria such as Escherichia coli and Salmonella Typhimurium. The results suggest that emu TENP is a potent novel antibacterial protein with a spectrum distinct from that of BPI.

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Section: ■ Results and Discussionmentioning

confidence: 68%

Biochemical and Functional Characterization of Transiently Expressed in Neural Precursor (TENP) Protein in Emu Egg White

Maehashi

Ueda

Matano

et al. 2014

J. Agric. Food Chem.

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“…To determine the partial amino acid sequences of sample proteins, in-gel digestion was performed following the method of Cleveland et al using Staphylococcus aureus V8 protease (Wako Pure Chemical Industries, Ltd., Osaka, Japan) as described in our previous paper . After electroblotting on a PVDF membrane (Bio-Rad, Hercules, CA), each separated band of a proteolytic fragment was excised from the membrane and subjected to a protein sequencer PPSQ-21 (Shimazdu, Kyoto, Japan) for amino (N)-terminal analysis.…”

Section: Methodsmentioning

confidence: 99%

Primary Structure of Potential Allergenic Proteins in Emu (Dromaius novaehollandiae) Egg White

Maehashi¹,

Matano²,

Irisawa³

et al. 2010

J. Agric. Food Chem.

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The emu (Dromaius novaehollandiae) egg is considered promising as an alternative egg product. To obtain basic biochemical information on emu egg white, the major protein compositions in emu and chicken egg whites and the primary structures of potential allergenic proteins were compared. The dominant protein in emu egg white was ovotransferrin (OVT), followed by ovalbumin (OVA) and TENP protein. The OVA and ovomucoid (OVM) levels in emu egg white were estimated as significantly lower than those in chicken egg white by Western blotting and enzyme-linked immunosorbent assays using anti-chicken OVA or OVM antibodies. Lysozyme and its enzymatic activity were not detected in emu egg white. OVT, OVA, and OVM genes were also cloned, and their nucleotide and amino acid sequences were determined. The protein sequences of OVT, OVA, and OVM from emu showed lower similarities to those of chicken than other avian species, such as quail and turkey. These results emphasize the low allergenicity of emu egg white and its potential as an alternative to chicken egg white.

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“…So far, the protein has been identified in other oviparous species in addition to chicken (Maehashi et al 2009), amphibian (Storey et al 1999), fish (Wang et al 2003), and mammals (Natraj et al 1988). In ovipara, the RfBP gene is expressed in the liver and the oviduct in an estrogen-dependent manner, and in oocytes subsequent to fecundation (Hamajima and Ono 1995;Zheng et al 1988;Maehashi et al 2009). The estrogen-dependent and fecundation-induced expression patterns are also found in other animals (Storey et al 1999;Natraj et al 1988;Wang et al 2003).…”

Section: Introductionmentioning

confidence: 95%

Down-regulation of free riboflavin content induces hydrogen peroxide and a pathogen defense in Arabidopsis

Deng

Sun

et al. 2011

Plant Mol Biol

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Riboflavin mediates many bioprocesses associated with the generation of hydrogen peroxide (H₂O₂), a cellular signal that regulates defense responses in plants. Although plants can synthesize riboflavin, the levels vary widely in different organs and during different stages of development, indicating that changes in riboflavin levels may have physiological effects. Here, we show that changing riboflavin content affects H₂O₂ accumulation and a pathogen defense in Arabidopsis thaliana. Leaf content of free riboflavin was modulated by ectopic expression of the turtle gene encoding riboflavin-binding protein (RfBP). The RfBP-expressing Arabidopsis thaliana (REAT) plants produced the RfBP protein that possessed riboflavin-binding activity. Compared with the wild-type plant, several tested REAT lines had >70% less flavins of free form. This change accompanied an elevation in the level of H₂O₂ and an enhancement of plant resistance to a bacterial pathogen. All the observed REAT characters were eliminated due to RfBP silencing (RfBPi) under REAT background. When an H₂O₂ scavenger was applied, H₂O₂ level declined in all the plants, and REAT no longer exhibited the phenotype of resistance enhancement. However, treatment with an NADPH oxidase inhibitor diminished H₂O₂ content and pathogen defense in wild-type and RfBPi but not in REAT. Our results suggest that the intrinsic down-regulation of free flavins is responsible for NADPH oxidase-independent H₂O₂ accumulation and the pathogen defense.

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The primary structure of a novel riboflavin-binding protein of emu (Dromaius novaehollandiae)

Cited by 6 publications

References 27 publications

Biochemical and Functional Characterization of Transiently Expressed in Neural Precursor (TENP) Protein in Emu Egg White

Biochemical and Functional Characterization of Transiently Expressed in Neural Precursor (TENP) Protein in Emu Egg White

Primary Structure of Potential Allergenic Proteins in Emu (Dromaius novaehollandiae) Egg White

Down-regulation of free riboflavin content induces hydrogen peroxide and a pathogen defense in Arabidopsis

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