Separation of Ovomucin Subunits by Gel Filtration:  Enhanced Resolution of Subunits by Using a Dual-Column System

Hiidenhovi, Jaakko; Aro, Heikki; Kankare, Veikko

doi:10.1021/jf9811774

Cited by 22 publications

(13 citation statements)

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“…Two components of α-ovomucin - α1 and α2-ovomucins with estimated molecular weights of 150 and 220 kDa respectively were reported [35] and another α-ovomucin component with molecular weight of 350 kDa was reported as well [39]. Our results confirmed the presence of β-ovomucin in the 350-400 kDa gel region, in agreement with previous reports [35,38].…”

Section: Discussionsupporting

confidence: 92%

“…α-ovomucin was present in gel bands that corresponded to molecular weights of~350 kDa and 250 kDa; however, it was not detected in 150 kDa region where the major protein was ovostatin. The absence of α1-ovomucin in the 160 kDa fraction obtained by gel filtration was reported previously [39]. However, LC-MS/MS analysis of egg white revealed α-ovomucin on SDS-PAGE gel in the area of 100-250 kDa [40].…”

Section: Discussionsupporting

confidence: 78%

“…Ovomucin, a glycoprotein responsible for the gel properties of fresh egg white, is composed of two components: β-ovomucin, with molecular weight of 400-610 kDa [35,38,39] and α-ovomucin -a polypeptide of 2087 amino acids with an estimated molecular mass of 254 kDa [9,37]. Two components of α-ovomucin - α1 and α2-ovomucins with estimated molecular weights of 150 and 220 kDa respectively were reported [35] and another α-ovomucin component with molecular weight of 350 kDa was reported as well [39].…”

Section: Discussionmentioning

confidence: 99%

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N-glycosylation of ovomucin from hen egg white

Offengenden

Fentabil

2011

Glycoconj J

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Ovomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. Our results showed the presence of N-linked glycans on both glycoproteins. We found 18 potential N-glycosylation sites in α-ovomucin. 15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). Two N-glycosylated sites were found in β-ovomucin.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionsupporting

confidence: 78%

Section: Discussionmentioning

confidence: 99%

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N-glycosylation of ovomucin from hen egg white

Offengenden

Fentabil

2011

Glycoconj J

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“…There are two types of ovomucin: a-and b-types (Hiidenhovi, Aro, & Kankare, 1999;Li-Chan, Powrie, & Nakai, 1995).…”

Section: Introductionmentioning

confidence: 99%

Enzymatic hydrolysis of ovomucin and the functional and structural characteristics of peptides in the hydrolysates

Abeyrathne

Lee

et al. 2016

Food Chemistry

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Ovomucin was hydrolyzed using enzymes or by heating under alkaline conditions (pH 12.0), and the functional, structural and compositional characteristics of the peptides in the hydrolysates were determined. Among the treatments, heating at 100 °C for 15 min under alkaline conditions (OM) produced peptides with the highest iron-binding and antioxidant capacities. Ovomucin hydrolyzed with papain (OMPa) or alcalase (OMAl) produced peptides with high ACE-inhibitory activity. The mass spectrometry analysis indicated that most of the peptides from OMPa were <2 kDa, but peptides from OMTr and OM were >2 kDa. OMAl hydrolyzed ovomucin almost completely and no peptides within 700-5000 Da were found in the hydrolasate. The results indicated that the number and size of peptides were closely related to the functionality of the hydrolysates. Considering the time, cost and activities of the hydrolysates, OM was the best treatment for hydrolyzing ovomucin to produce functional peptides.

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“…Mouse monoclonal (MAb59 and MAb66 IgG) and rabbit polyclonal (R290 IgG) antibodies against human PLTP were produced as described earlier ( 13 ). A soluble form of ovomucin was purifi ed from egg-white as described earlier ( 17 ).…”

Section: Protein Samples and Antibodiesmentioning

confidence: 99%

Interaction of phospholipid transfer protein with human tear fluid mucins

Setälä

Holopainen

Metso

et al. 2010

Journal of Lipid Research

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This article is available online at http://www.jlr.org well as an economic burden to patients and the community. DES is considered to arise from the interplay of inadequate tear production, increased tear evaporation, and altered composition of the tear fi lm. The underlying biochemical and physiological events in the development of DES and precise composition of the human tear fl uid are only partially understood. Until now the model of the tear fi lm has been a three-layered structure ( 2, 3 ): the inner mucin-enriched phase and the middle aqueous layer with soluble proteins form a gel-like structure while the outermost layer consists of lipids. On the basis of analysis of meibomian gland secretions, the lipid layer is suggested to be composed of wax esters, sterol esters, and polar lipids ( 4, 5 ). It has been suggested, based on the hydrophobic effect, that the charged (polar) phospholipids are disposed adjacent to the aqueous-mucin layer and, externally to this, a layer composed of nonpolar lipids, such as cholesteryl esters and triglycerides, face the tear-air interface (6)(7)(8). This type of lipid organization is believed to strongly oppose evaporation. Yet, the ocular and mucin components become vulnerable to lipid contamination, which would lead to dewetting of the corneal epithelium. A mechanism to organize and maintain homeostasis of the lipid layer and to prevent epithelial or mucin contamination is needed. Indeed, lipocalin, one such kind of protein, has been confi rmed to effi ciently remove lipids from the corneal surface ( 9 ). Yet this observation does not ex- Dry eye syndrome (DES), the most common ocular disorder that affects around 14% of individuals aged 65 ± 10 years ( 1 ), poses a considerable public health problem as Abbreviations: Apo, apolipoprotein; BSM, bovine submaxillary gland mucin; CETP, cholesteryl ester transfer protein; DES, dry eye syndrome; H-S, heparin-sepharose; MUC, mucin; OVM, ovomucin; PLTP, phospholipid transfer protein; SEC, size exclusion chromatography; Tlc, human tear lipocalin.

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Separation of Ovomucin Subunits by Gel Filtration: Enhanced Resolution of Subunits by Using a Dual-Column System

Cited by 22 publications

References 29 publications

N-glycosylation of ovomucin from hen egg white

N-glycosylation of ovomucin from hen egg white

Enzymatic hydrolysis of ovomucin and the functional and structural characteristics of peptides in the hydrolysates

Interaction of phospholipid transfer protein with human tear fluid mucins

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