Purification and some properties of thiamine-binding protein from rice bran.

Nishimura, Hiroshi; Uehara, Yasuo; Sempuku, Kenji; Iwashima, Akio

doi:10.3177/jnsv.30.1

Cited by 24 publications

(16 citation statements)

References 13 publications

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“…The thiamin binding of STBPs was not inhibited by thiamin monophosphate (TMP), thiamin pyrophosphate (TMPP) or oxythiamin (Table 1), which was also the case with the TBPs from other plant seeds (Nishimura et al 1984a; Mitsunaga et al 1986). However, the thiamin binding of STBPs was inhibited by pyrithiamin, in contrast with the case of the TBPs from other plant seeds (Nishimura et al 1984a; Mitsunaga et al 1986). The 10‐fold molar concentration of pyrithiamin reduced the thiamin binding of STBPs to 11–17%.…”

Section: Resultsmentioning

confidence: 85%

“…The 10‐fold molar concentration of pyrithiamin reduced the thiamin binding of STBPs to 11–17%. This showed that pyrithiamin bound to STBPs in the same manner as thiamin (Iwashima et al 1979; Nishimura et al 1984a).…”

Section: Resultsmentioning

confidence: 89%

“…Thiamin‐binding proteins (TBPs) found in plant seeds bind only free thiamin and are assumed to be seed storage proteins because of their localization in plant seeds (Nishimura et al 1984a), although the TBPs from microorganisms and animal tissues bind both free thiamin and thiamin phosphates and are involved in thiamin transport (Iwashima et al 1979; Muniyamppa and Adiga 1979). Sesame seeds have two 17‐kDa TBPs, termed STBP‐I and ‐II, and a 19‐kDa TBP, termed STBP‐III (Shimizu et al 1995).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Properties of thiamin‐binding proteins from sesame seed 2S albumins

Watanabe

Chikushi

Adachi

et al. 1999

Physiologia Plantarum

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Three thiamin‐binding proteins (TBPs) from sesame (Sesamum indicum L.) seeds (STBP‐I, ‐II and ‐III) were characterized. Binding of thiamin to the three STBPs was inhibited by pyrithiamin, which did not inhibit the binding of thiamin to TBPs from other plant seeds. STBP‐I alone bound 2‐northiamin and hydroxyethylthiamin. Isoelectric points (pIs) of STBP‐I and ‐II both were 7.5. The pI of STBP‐III was 6.5. STBPs did not have immunological homology with TBPs from rice seeds and buckwheat seeds. On the other hand, the amino acid compositions of the small and large polypeptides isolated from STBP‐I, ‐II and ‐III resembled each other. Both the polypeptides contained large amounts of Glu (or Gln) and Arg. The small polypeptides contained more Ser than the large polypeptides. The N‐terminal amino acid sequences (the first 29 residues) of the small polypeptides were identified. The N‐terminal amino acid sequences of the three STBPs were the same. The small polypeptides had homology to castor bean 2S albumin small subunit. These results showed that STBPs were part of a plant protein superfamily and that STBPs differed from the TBPs of other plant seeds as to the binding to thiamin‐related compounds and immunological properties, and further, that STBP‐I, ‐II and ‐III differed in the affinity for thiamin‐related compounds and pI, indicating that STBP‐I, ‐II and ‐III are isomers.

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Section: Resultsmentioning

confidence: 85%

Section: Resultsmentioning

confidence: 89%

Section: Introductionmentioning

confidence: 99%

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Properties of thiamin‐binding proteins from sesame seed 2S albumins

Watanabe

Chikushi

Adachi

et al. 1999

Physiologia Plantarum

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“…The optimum pH for the thiamin-binding activity of the TBP from sunflower Vo1 44, No 5, 1998 seeds was pH 8 to 9, where the TBPs from buckwheat seeds and rice seeds also exhibit maximum activity (1,3). In contrast, the thiamin-binding activity of the TBP from sesame seeds is maximum in the pH 6 to 8 region (2).…”

Section: Discussionmentioning

confidence: 99%

Thiamin-Binding Protein from Sunflower Seeds.

Watanabe

Chikushi

Adachi

et al. 1998

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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SummaryA thiamin-binding protein was isolated from sunflower seeds. Its molecular mass was estimated to be 230 kDa by gel filtration. The protein was suggested to be composed of six subunits, which con sisted of polypeptides linked by disulfide bond(s). The protein contained a large amount of glutamine or glutamic acid (19.9 mol%) and aspa ragine or aspartic acid (11.1 mol%). The levels of tryptophan and valine in the protein were low. These properties of the thiamin-binding protein were similar to those of helianthinin. Optimum pH for the thiamin-binding activity of the protein was 8.0 to 9.0. The thiamin-binding activity was not inhibited by thiamin monophosphate, thiamin pyrophosphate, oxy thiamin, or pyrithiamin. These properties of the thiamin-binding protein from sunflower seeds were similar to those from buckwheat seeds, but not to those from rice seeds and sesame seeds. Key Words seed, storage protein, sunflower, thiamin, thiamin-binding protein Plant seeds contain thiamin-binding proteins (TBPs) that specifically bind free thiamin, but not thiamin phosphates (1). The TBPs are assumed to retain thiamin, which is accumulated into dormant seeds for germination, and the proteins are degraded to supply thiamin and a nitrogen source during germination (2). TBPs having such dual functions are novel storage proteins because, in general, storage proteins have no functions except to provide nitrogen sources during germination. However, only TBPs from sesame seeds, rice seeds and buckwheat seeds have been characterized (1-5). The results indicate that these TBPs differ in molecular weight and subunit structure, amino acid composition, optimum pH for thiamin-binding activity, and binding activity for thiamin analogs, although the TBPs are found only in seeds and specifically bind free thiamin, but not thiamin phosphates. The

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“…Several TPP binding proteins from microbial organisms, higher plants and animals have already been described [27]. The K D values range between 1.1*10 -6 M and 2.8*10 -8 M [28][29][30][31][32].…”

Section: Affinity Separation With Crude Cell Brothmentioning

confidence: 99%

Comparison of Purification Efficiencies of Different Affinity Separation Techniques

Koetke¹

2010

toacj

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An affinity separation method for the isolation of recombinantly produced benzoylformiate decarboxylase (BFD) is presented based on the interaction of the enzyme to its cofactor. Enzyme/cofactor interactions are well suited for affinity purification processes with regard to its high affinity and selectivity. Problems can be induced due to harsh desorption conditions that probably diminish the activity of the purified enzyme. The implementation of boronic acids to immobilize the cofactor introduces a gentle release by a simple pH shift from 8.5 to 6. The disadvantages of maminophenyl boronic acids are the high nonspecific adsorption induced by the introduction of a positive charge and a hydrophobic phenyl ring. It was shown that the disadvantages prevail and boronic acid resins are not suitable for protein purification from complex matrices. In contrast to the affinity separation method, where the cofactor was directly immobilized onto the support, a better separation performance could be achieved, which is reflected by a purification factor of 4.

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Purification and some properties of thiamine-binding protein from rice bran.

Cited by 24 publications

References 13 publications

Properties of thiamin‐binding proteins from sesame seed 2S albumins

Properties of thiamin‐binding proteins from sesame seed 2S albumins

Thiamin-Binding Protein from Sunflower Seeds.

Comparison of Purification Efficiencies of Different Affinity Separation Techniques

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