Structural characterization of a rhamnose-binding glycoprotein (lectin) from Spanish mackerel (Scomberomorous niphonius) eggs

Terada, Takatomo; Watanabe, Yoshifumi; Tateno, Hiroaki; Naganuma, Takako; Ogawa, Tomoya; Muramoto, Koji; Kamiya, Hisao

doi:10.1016/j.bbagen.2006.11.003

Cited by 66 publications

(46 citation statements)

References 30 publications

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“…All cysteines are oxidized and the S-S-bond pattern is symmetrical across the tandem-repeat sequence, which is consistent with the related rhamnose-binding egg lectins from the Spanish mackerel [24,25].…”

Section: Assignment Of the Disulfide Bond Pattern In Sel24ksupporting

confidence: 80%

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Gas-phase scrambling of disulfide bonds during matrix-assisted laser desorption/ionization mass spectrometry analysis

Zhao¹,

Almaraz

Fan

et al. 2009

J. Am. Soc. Mass Spectrom.

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Evidence for photo-induced radical disulfide bond scrambling in the gas phase during matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is described. The phenomenon was observed during the analysis of tryptic peptides from insulin and was confirmed in the determination of disulfide bonds in the rhamnose-binding lectin SEL24K from the Chinook salmon Oncorhynchus tshawytscha. A possible mechanism for this surprising scrambling is proposed. Despite this finding, the disulfide bond pattern in SEL24K was assigned unambiguously by a multi-enzyme digestion strategy in combination with MALDI mass spectrometry. The pattern was found to be symmetrical in the tandem repeat sequence of SEL24K. To the best of our knowledge, this is the first report of disulfide bond scrambling in the gas phase during MALDI-MS analysis. This observation has important ramifications for unambiguous assignment of disulfide bonds. (J Am Soc

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Section: Assignment Of the Disulfide Bond Pattern In Sel24ksupporting

confidence: 80%

“…Finally, it is interesting to notice that in related rhamnose-binding lectins from the Spanish mackerel [24], peptides generated by trypsin have typically only one disulfide bond so that gas-phase scrambling is not of concern in this case, and ISD analysis remains a valuable analytical technique.…”

Section: Gas-phase Scrambling Of Disulfide Bonds In Sel24kmentioning

confidence: 99%

Gas-phase scrambling of disulfide bonds during matrix-assisted laser desorption/ionization mass spectrometry analysis

Zhao¹,

Almaraz

Fan

et al. 2009

J. Am. Soc. Mass Spectrom.

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“…35,38,[40][41][42] Three RBLs, named STL1, STL2, and STL3, were isolated from eggs of steelhead trout (Oncorhynchus mykiss) 41,42 and three RBLs, CSL1, CSL2, and CSL3, with a high degree of sequence identity with O. mykiss were isolated from chum salmon (Oncorhynchus keta) 43 (Table 18.1). Only one RBL (SAL) and two RBLs (WCL1 and WCL3) were isolated from catfish (Silurus asotus) and whitespotted charr (Salvelinus leucomaenis) eggs, respectively 44,45 (Table 18.1).…”

Section: Rbls In Fish: Biochemical and Molecular Featuresmentioning

confidence: 99%

“…36,37 RBLs share the presence of one or multiple CRDs with a unique β/β fold, about 100 amino acid in length, with 8 highly conserved cysteine residues engaged in 4 disulfide bridges with characteristic topology. 22,38,39 In addition, conserved motifs (YGR, DPC, and KYL) are also found. 38 …”

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confidence: 95%

Evolution and Immune Function of Fish Lectins

Cammarata¹,

Parisi²,

Vasta³

2016

Lessons in Immunity

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Any queries or remarks that have arisen during the processing of your manuscript are listed below and are highlighted by flags in the proof. (AU indicates author queries; ED indicates editor queries; and TS/TY indicates typesetter queries.) Please check your proof carefully and answer all AU queries. Mark all corrections and query answers at the appropriate place in the proof using on-screen annotation in the PDF file. For a written tutorial on how to annotate PDFs, click http://www.elsevier.com/__data/assets/ pdf_file/0007/98953/Annotating-PDFs-Adobe-Reader-9-X-or-XI.pdf. A video tutorial is also available at http://www.screencast. com/t/9OIDFhihgE9a. Alternatively, you may compile them in a separate list and tick off below to indicate that you have answered the query. Please return your input as instructed by the project manager. Location in articleQuery / remark AU1, page 244 Please provide the expansion for genus names "S. purpuratus" and "C. intestinalis" in the sentence "In contrast, the N…". ■ AU4, page 250 Please check the term "conCL-s" mentioned in the sentence "In the latter, conCL-s…". ■ AU5, page 243The citation 'Ogawa et al.,25 ' in the legend of To protect the rights of the author(s) and publisher we inform you that this PDF is an uncorrected proof for internal business use only by the author(s), editor(s), reviewer(s), Elsevier and typesetter TNQ Books and Journals Pvt Ltd. It is not allowed to publish this proof online or in print. This proof copy is the copyright property of the publisher and is confidential until formal publication. 10018-BALLARIN-9780128032527Chapter 18 Evolution and Immune Function of Fish LectinsMatteo Cammarata, Maria G. Parisi University of Palermo, Palermo, Italy Gerardo R. Vasta University of Maryland School of Medicine, Baltimore, MD, United States c0018 INTRODUCTIONThe term "lectin" is commonly used to encompass a wide variety of carbohydrate-binding proteins, widely distributed in viruses, prokaryotes, and eukaryotes. 1 The first invertebrate lectins were described in the early 1900s in the snail Helix pomatia, 2 the horseshoe crab Limulus polyphemus, 3 and the lobster Homarus americanus. 3 Among the vertebrates, Watkins and Morgan 4 first described an l-fucose-specific lectin in the European eel Anguilla anguilla, which led to the discovery of the carbohydrate nature of the H blood substance. Animal lectins are grouped in various molecular families, differing in carbohydrate recognition domain (CRD) structure and organization. 1,[5][6][7] Based on their CRD sequence motifs and cation requirements, animal lectins can be categorized in several families, such as C-type lectins (CTLs), galectins (formerly S-type lectins), rhamnose-binding lectins (RBLs), F-type lectins (FTLs), X-type lectins (XTLs), I-type lectins, P-type lectins, and pentraxins. 1,[5][6][7] Lectins are involved in a variety of key biological processes ranging from development to immune responses. 1,[7][8][9][10][11] The roles of lectin-carbohydrate interactions in self/non-self recognition in early dev...

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“…These processing will produce a lot of byproducts, including head, skin, frame, viscera and others, which occupy about 50% of total weight and mainly are used for animal feeds (Cho et al, 2014). However, these mackerel processing byproducts are enriched in protein and maybe valuable source of bioactive peptides or functional foods ingredients, such as fish oil (Sahena et al, 2010), antibacterial peptides (Ennaas et al, 2015), gelatin (Khiari et al, 2011), rhamnose-binding glycoprotein (Terada et al, 2007), iron-binding peptides and polyunsaturated fatty acids (Zuta et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Stability of Mackerel (Trachurus japonicas) Hydrolysate with Iron-Binding Capacity in Simulated Gastrointestinal Fluids

Zhang¹,

Sun²,

Huang³

2015

American J. of Food Technology

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The aim of this study was to investigate the stability of mackerel (Trachurus japonicas) processing byproducts protein hydrolysate with iron-binding capacity in vitro simulated gastrointestinal systems. The changes in molecular weight distribution and iron-binding capacity were used for evaluating the stability of the hydrolysate in simulated gastrointestinal digestion. The molecular weight of mackerel hydrolysate with iron-binding capacity was mostly less than 1300 Da and composted mainly by tripeptides to undepeptides. The hydrolysate was stable in gastric or intestinal digestion separately for 5 h, or two-stage gastrointestinal digestion. The iron-binding capacity did not change significantly during gastrointestinal digestion. The mackerel processing byproducts hydrolysate had potential in iron fortification functional ingredients of food industry.

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Structural characterization of a rhamnose-binding glycoprotein (lectin) from Spanish mackerel (Scomberomorous niphonius) eggs

Cited by 66 publications

References 30 publications

Gas-phase scrambling of disulfide bonds during matrix-assisted laser desorption/ionization mass spectrometry analysis

Gas-phase scrambling of disulfide bonds during matrix-assisted laser desorption/ionization mass spectrometry analysis

Evolution and Immune Function of Fish Lectins

Stability of Mackerel (Trachurus japonicas) Hydrolysate with Iron-Binding Capacity in Simulated Gastrointestinal Fluids

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