Determination of the carbohydrate composition and the disulfide bond linkages of bovine lactoperoxidase by mass spectrometry

Wolf, Susan M.; Ferrari, Rosa Pia; Traversa, Silvio; Biemann, K.

doi:10.1002/(sici)1096-9888(200002)35:2<210::aid-jms931>3.0.co;2-z

Cited by 35 publications

(34 citation statements)

References 26 publications

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“…However, as LPS is a glycoprotein that contains almost 10% carbohydrate, such an heterogeneity may also be related to the type of carbohydrate attached to the enzyme by glycosylation. In fact, Wolf, Ferrari, Traversa, and Biemann (2000) reported that the glycosylation sites of LPS are fully occupied with different high mannose and complex structures and this may vary molecular weight of LPS between 74,850 and 79,188 Da.…”

Section: Partial Purification Of Lpsmentioning

confidence: 99%

Partial purification and preparation of bovine lactoperoxidase and characterization of kinetic properties of its immobilized form incorporated into cross-linked alginate films

Mecitoğlu

Yemenicioğlu

2007

Food Chemistry

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Lactoperoxidase (LPS), purified directly from bovine rennet whey by Toyopearl-SP cation-exchange chromatography and lyophilized by using dextran as supporting material, maintained almost 70 and 60% of its activity after almost 2 and 5 months storage at À18°C, respectively. Incorporation of the prepared LPS into alginate films between 0.08 and 0.69 mg/cm 2 (516-4325 U/cm 2 ) caused the immobilization of most of the enzyme and gave films with LPS activity between 0.05 and 2.8 U/cm 2 , determined in the presence of 8 lM H 2 O 2 . Between 2 and 24 lM H 2 O 2 concentrations, a two-fold increase in H 2 O 2 concentration caused 1.5-2.5-fold increase in LPS activity of films incorporated with 0.24-0.28 mg/cm 2 (1200 U/cm 2 ) LPS. The Q 10 and E a of immobilized enzyme activity between 4 and 16°C were 1.69 and 34.6 kJ/mol, respectively. However, in the 16-30°C range, the temperature change had almost no effect on LPS activity of films. The optimal activity of immobilized LPS was observed at pH 6.0, but the enzyme maintained 30-85% of its activity between pH 3.0 and 7.0. The immobilized LPS also had a high stability between pH 4.0 and 6.0. The results of this study showed the good potential of LPSincorporated alginate films in forming a natural antimicrobial mechanism in different foods.

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Section: Partial Purification Of Lpsmentioning

confidence: 99%

Partial purification and preparation of bovine lactoperoxidase and characterization of kinetic properties of its immobilized form incorporated into cross-linked alginate films

Mecitoğlu

Yemenicioğlu

2007

Food Chemistry

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“…Using this strategy, it has been shown that the nonoccupancy of the three glycosylation sites in a plasma protein, α1-antitrypsin, from CDG-I patients was not random but determined by structural features [89,90]. A similar strategy has also been successfully used to determine the extent and distribution of N-glycosylation in bovine lactoperoxydase [91].…”

Section: A Mald-msmentioning

confidence: 99%

Glycomics and Mass Spectrometry

Morelle¹,

Michalski

2005

CPD

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Proteomics is closely associated with the modifications of the gene product such as the post-translational events that yield functionally active gene products. Among these, glycosylation represents a critically important post-translational modification and is a target for proteomic research. Glycan moieties are involved in a wide variety of intracellular, cell-cell and cell-matrix recognition events. This is why understanding how glycosylation affects the activities and functions of proteins in health and disease represents a major challenge. The study of the glycome--the whole set of glycans produced in a single organism--is therefore essential to determine the functions of all genes. Mass spectrometry, in combination with modern separation methodologies, is one of the most powerful and versatile techniques for the structural analysis of oligosaccharides. This review provides a summary of the current knowledge for the mass spectrometric analysis of glycoproteins and their glycan structures.

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“…One of those compounds is the enzyme lactoperoxidase. [14] Lactoperoxidase (LPO; EC 1.11.1.7) is a heme-containing glycoprotein with a single chain of 612 residues. LPO contains about 10% carbohydrate and its molecular mass is approximately 78 kDa.…”

Section: Introductionmentioning

confidence: 99%

The Inhibitory Effects of L-Adrenaline on Lactoperoxidase Enzyme Purified from Bovine Milk

Şişecioğlu

Gülçın

Çankaya

et al. 2012

International Journal of Food Properties

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L-Adrenaline belongs to a group of compounds known as catecholamines, which play an important role in the regulation of the physiological process in living organisms. In the present study, the inhibitory effect of L-adrenaline on lactoperoxidase was examined. Lactoperoxidase (E.C.1.11.1.7) was purified from bovine milk with three consecutive steps: Amberlite CG-50 resin, CM-Sephadex C-50 ion-exchange, and Sephadex G-100 gel filtration chromatography. Lactoperoxidase was purified with a yield of 42.18%, a specific activity of 30.33 EU/mg proteins, and 20.77 purification fold. Enzyme purity was determined with SDS-PAGE, where a single band was observed. The R z (A 412 /A 280 ) value for lactoperoxidase was 0.9. The effect of L-adrenaline on lactoperoxidase was determined using ABTS as a chromogenic substrate. The half maximal inhibitory concentration (IC 50 ) value and an inhibition constant (K i ) values for L-adrenaline were 34.5 and 2.26 µM, respectively. L-Adrenaline was found to be a non-competitive inhibitor.

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Determination of the carbohydrate composition and the disulfide bond linkages of bovine lactoperoxidase by mass spectrometry

Cited by 35 publications

References 26 publications

Partial purification and preparation of bovine lactoperoxidase and characterization of kinetic properties of its immobilized form incorporated into cross-linked alginate films

Partial purification and preparation of bovine lactoperoxidase and characterization of kinetic properties of its immobilized form incorporated into cross-linked alginate films

Glycomics and Mass Spectrometry

The Inhibitory Effects of L-Adrenaline on Lactoperoxidase Enzyme Purified from Bovine Milk

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