Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene

Byrne, Barry; Schip, AD van het; Klundert, J. A. M. Van De; Arnberg, Annika C.; Gruber, M.; Ab, Geert

doi:10.1021/bi00314a003

Cited by 147 publications

(97 citation statements)

References 29 publications

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“…The shape of the curve implies that phosvitin (and polynucleotides) forms a ternary complex ('template') with binding to both HCII and thrombin. The binding sites for HCII and thrombin probably reside in the phosphoserine-rich core region of phosvitin [20]. This is the first demonstration that a protein or a polynucleotide, not a glycosaminoglycan like heparin or dermatan sulfate, can serve as a surface (or template) for thrombin inhibition by a proteinase inhibitor.…”

Section: Discussionmentioning

confidence: 83%

Antithrombin action of phosvitin and other phosphate‐containing polyanions is mediated by heparin cofactor II

et al. 1988

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We have examined the antithrombin effects of various phosphate-containing polyanions (including linear polyphosphates, polynucleotides and the phosphoserine glycoprotein, phosvitin) on the glycosaminoglycan-binding plasma proteinase inhibitors, antithrombin III (ATIII) and heparin cofactor II (HCII). These phosphate-containing polyanions accelerate the HCII-thrombin reaction, as much as 1600-fold in the case of phosvitin. The HCII-thrombin reaction with both phosvitin and polynucleotides appears to follow the ternary complex mechanism. The HCII-thrombin complex is rapidly formed in the presence of these phosphate polyanions (each at 10 fig/ml) when 'ZSI-labeled thrombin is incubated with human plasma (ex vivo). None of these phosphate polyanions accelerate the ATIII-thrombin reaction. Our results suggest that the antithrombotic effect of these phosphate-containing polyanions is mediated by HCII activation and not by ATIII.

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Section: Discussionmentioning

confidence: 83%

Antithrombin action of phosvitin and other phosphate‐containing polyanions is mediated by heparin cofactor II

et al. 1988

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“…Sodium hydroxide can hydrolyze phosphor ester bond effectively so as to achieve the purpose of dephosphorization. bonds not easily to be functioned by protease (Goulas et al, 1996;Byrne et al, 1984). During the process of dephosphorization, the changes of structure in the core area make it subject to enzyme (Jiang et al, 2000).…”

Section: Resultsmentioning

confidence: 99%

Purification of a Novel Oligophosphopeptide with High Calcium Binding Activity from Carp Egg Hydrolysate

Huang

Liu

et al. 2014

FSTR

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Keywords: purification, carp eggs, hydrolysate, dephosphorization, calcium binding activity, oligophosphopeptide IntroductionThe global fishery production reached 178 million tons in 2011(i), more than 50% of which was discarded as inedible byproducts such as bone, skin, internal organs, head and eggs (Jung et al., 2005). Plentiful research have been implemented on utilizing fishery byproducts (Chakraborty et al., 2011;Duan et al., 2009;Kongsri et al., 2013;Mori et al., 2013). However, the utilization studies on eggs, especially on freshwater fish eggs, are very scarce.Eggs are rich in lipids (especially phospholipids and n-3 polyunsaturated fatty acids), the yolk protein, mineral elements, vitamins, carotenoids, and other nutrients. But in the conventional process, eggs are often treated as waste to be abandoned. AbbreviationsCPP; casein phosphopeptide, Hy; carp egg tryptic hydrolysate, DP0; carp eggs without dephosphorization, DP1, DP2, DP3, and DP4; dephosphorized carp eggs with degree of dephosphorization of 13.66%, 30.39%, 48.71%, and 83.49% respectively, U1 and U2; the fractions after ultrafiltration with molecular weight <3 kDa and > 3 kDa respectively, H1, H2 and H3; the fractions eluted with 100 mM, 200 mM and 400 mM phosphate buffer respectively on hydroxyapatite chromatography column, HA; hydroxyapatite chromatography H. Huang et al. 800 Calcium is an important mineral element to maintain human health, which plays an important role in the formation of bones and teeth, neurotransmitter release, muscle composition, and heart beat regulation. Calcium is mainly ingested through drinks and food, especially milk or cheese products with high calcium content. Influenced by lactose intolerance, dietary habits, and other factors,Asians intake less milk and cheese products and their food mainly focuses on vegetable diet. However, substances such as the phytic acid, oxalic acid, saturated fatty acids, and dietary fiber are easily combined with calcium to form insoluble matter, which is not beneficial to calcium absorption.Many peptides isolated from animals possessed the ability of binding Ca Lee et al., 2009;Jiang et al., 2000;Jung et al., 2007). Casein phosphopeptides (CPPs) were well known for their metal binding abilities because the CPPs contained electronegative phosphoserines (West et al., 1986;Meisel et al., 1990;Yuan et al., 1991;Gerber et al., 1986;Sato et al., 1986). The phosphopeptides obtained from the enzymolysis of fish bone (Jung et al., 2007(Jung et al., , 2006(Jung et al., , 2005 can also chelate Ca, whose performance is similar to CPPs. Many studies indicated that fish eggs also contain high phosphoprotein and can obtain phosphopeptides by hydrolysis (Catherine et al., 2002;Inoue et al., 1971).Carp was one of the most productive (over 3.8 million tons ) freshwater fish species in the world (ii). In breeding season, the ovarian can weigh 10% to 25.81% of the overall weight. In the present study, we will discuss the appropriate degree of dephosphorization of carp eggs before trypsin hydrolysi...

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“…( [8] If one assumes that, at antigen excess, the interaction between the homopolyvalent Ag (phosvitin) and where K d , the dissociation constant, is the reciprocal the mAb (anti-phosphoserine) is in monovalent mode, of the association constant K b and c is the total Ag Whitesides' equation (1) The migration time (t) of the mAb or mAb-Ag complexes was first corrected to a fixed value of the migra- The Ag (phosvitin) at various concentrations was Phosvitin (pI 2.1) contains a ratio of serine to all first incubated in solution with the mAb (anti-phosphoother amino acid residues of 3:2 and is phosphorylated serine) at a constant concentration until equilibrium on the multiple-site serine residues (35). It thus exhibwas reached.…”

Section: Fig 1 Schematic Diagram Depicting the Interaction Of Monocmentioning

confidence: 99%

Determination of the Dissociation Constant of Phosvitin–Anti-phosphoserine Interaction by Affinity Capillary Electrophoresis

Lin

Hsiao

Hsu

1997

Analytical Biochemistry

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Amino acid sequence of phosvitin derived from the nucleotide sequence of part of the chicken vitellogenin gene

Cited by 147 publications

References 29 publications

Antithrombin action of phosvitin and other phosphate‐containing polyanions is mediated by heparin cofactor II

Antithrombin action of phosvitin and other phosphate‐containing polyanions is mediated by heparin cofactor II

Purification of a Novel Oligophosphopeptide with High Calcium Binding Activity from Carp Egg Hydrolysate

Determination of the Dissociation Constant of Phosvitin–Anti-phosphoserine Interaction by Affinity Capillary Electrophoresis

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