Isolation and properties of flavoprotein from the egg yolk

Ostrowski, W; Skarzynski, B; Z, Zák

doi:10.1016/0006-3002(62)90217-2

Cited by 32 publications

(11 citation statements)

References 8 publications

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“…It is now well established that the binding proteins specific for riboflavin (Ostrowski et al, 1962;Murthy & Adiga, 1978), biotin (White et al, 1976) and iron (Williams, 1962) are present in both the yolk and the white of the chicken egg; although they are fully saturated with their respective ligands in the yolk, they occur primarily as apoproteins in the white (Feeney & Allison, 1969). The less lipoidal egg white was preferred as the starting material in view of the fact that thiamin in the egg is almost exclusively localized in the yolk (Long, 1961), and the technique of affinity chromatography on immobilized thiamin was the method ofchoice in our first attempts towards the isolation of the putative thiamin-binding protein.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of thiamin-binding protein from chicken egg white

Muniyappa¹,

Adiga²

1979

Biochemical Journal

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A thiamin-binding protein was isolated and characterized from chicken egg white by affinity chromatography on thiamin pyrophosphate coupled to aminoethyl-Sepharose. The high specificity of interaction between the thiamin-binding protein and the riboflavin-binding protein of the egg white, with a protein/protein molar ratio of 1.0, led to the development of an alternative procedure that used the riboflavin-binding protein immobilized on CNBr-activated Sepharose as the affinity matrix. The thiamin-binding protein thus isolated was homogeneous by the criteria of polyacrylamide-gel disc electrophoresis, double immunodiffusion and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, had a mol.wt. of 38,000 +/- 2000 and was not a glycoprotein. The protein bound [14C]thiamin was a molar ratio of 1.0, with dissociation constant (Kd) 0.3 micrometer.

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Section: Discussionmentioning

confidence: 99%

Isolation and characterization of thiamin-binding protein from chicken egg white

Muniyappa¹,

Adiga²

1979

Biochemical Journal

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“…The riboflavin carrier protein (RCP) is not a membrane-spanning carrier but a soluble protein that binds RF; however, the exact role in storing and transporting RF is still unknown. RCP was first identified in oviparous species in the 1960s [23,24]. Chicken RCP (cRCP) has been extensively investigated, as it is easy to isolate and purify in large quantities.…”

Section: Riboflavin Carrier Proteinmentioning

confidence: 99%

Riboflavin-Targeted Drug Delivery

Darguzyte

Drude

Lammers

et al. 2020

Cancers

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Active targeting can improve the retention of drugs and drug delivery systems in tumors, thereby enhancing their therapeutic efficacy. In this context, vitamin receptors that are overexpressed in many cancers are promising targets. In the last decade, attention and research were mainly centered on vitamin B9 (folate) targeting; however, the focus is slowly shifting towards vitamin B2 (riboflavin). Interestingly, while the riboflavin carrier protein was discovered in the 1960s, the three riboflavin transporters (RFVT 1-3) were only identified recently. It has been shown that riboflavin transporters and the riboflavin carrier protein are overexpressed in many tumor types, tumor stem cells, and the tumor neovasculature. Furthermore, a clinical study has demonstrated that tumor cells exhibit increased riboflavin metabolism as compared to normal cells. Moreover, riboflavin and its derivatives have been conjugated to ultrasmall iron oxide nanoparticles, polyethylene glycol polymers, dendrimers, and liposomes. These conjugates have shown a high affinity towards tumors in preclinical studies. This review article summarizes knowledge on RFVT expression in healthy and pathological tissues, discusses riboflavin internalization pathways, and provides an overview of RF-targeted diagnostics and therapeutics.

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“…The pH of the protein solution was adjusted to 3.0 and filtered through a column (1.5cmx20cm) of Sephadex G-25 with 0.1 M-sodium citrate buffer, pH3.0, as eluent, to separate the yellow flavin from the apoprotein (Ostrowski et al, 1962).…”

Section: Separation Oftheflavin From the Apoproteinmentioning

confidence: 99%

“…Riboflavin-Vol. 170 binding protein was isolated in a homogeneous form from egg white (Murthy & Adiga, 1977a) and egg yolk (Ostrowski et al, 1962), and a monospecific antibody against the egg-white riboflavin-binding protein was raised in rabbits as described elsewhere (Murthy et al, 1976). Florisil was obtained through Sigma Chemical Co., St. Louis, MO, U.S.A.…”

mentioning

confidence: 99%