Sequencing of cDNA Clones that Encode Bovine Ferritin H and L Chains

Orino, Koichi; Eguchi, Kohtaro; Nakayama, Takao; Yamamoto, Sinji; Watanabe, Kiyotaka

doi:10.1016/s0305-0491(97)00277-0

Cited by 36 publications

(34 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The commercial ferritin was almost entirely composed of L subunits, and the L/H subunit ratios of the purified horse spleen, canine liver, and bovine spleen ferritins were 4.0, 2.3 and 1.1, respectively, these results are in agreement with those in previous reports [17,18,30]. Apoferritins were prepared from each of the above ferritins using a reducing reagent as described previously [18].…”

Section: Binding Of Mammalian Holo-and Apoferritins With Biotinylatedsupporting

confidence: 81%

“…The designation of H(eart) and L(iver) types has been changed to the H(eavy) and L(ight) subunits based on their electric mobilities [29]. However, the terminology of ferritin subunits from the electrophoretic mobility provided some confusion from the unusual mobilities [2,17], and the characterization of subunit types may be uncertain without genetic, immunological or amino acid sequencing data [2,17]. Additionally, birds are known to express only an H subunit [3,14,22,28].…”

mentioning

confidence: 99%

“…Ferritin and apoferritin preparation: Horse spleen ferritin monomers were purified from commercial horse spleen ferritin as described previously [20]. Horse spleen, bovine spleen, and canine liver ferritin monomers were purified from pieces of frozen horse spleen, bovine spleen and canine liver, respectively, as described previously [13,17,18]. Chicken liver ferritin monomers were also purified from pieces of frozen pooled livers according to the method described previously [13] with minor modifications.…”

mentioning

confidence: 99%

“…Commercial horse spleen, horse spleen ferritin, bovine spleen and canine liver apoferritins were prepared by dialysis of their holoferritins with 100 mM thioglycolic acid in 100 mM acetate buffer (pH 5.5) followed by phosphate-buffered saline (PBS, 150 mM NaCl, 20 mM sodium phosphate, pH 7.2). Recombinant bovine H-and L-subunit homopolymers were obtained by expression of bovine ferritin H-and Lsubunit cDNAs using a baculovirus expression system with Spodoptera frugiperda as described previously [17,18].…”

mentioning

confidence: 99%

See 3 more Smart Citations

Binding of Mammalian and Avian Ferritins with Biotinylated Hemin: Demonstration of Preferential Binding of the H Subunit to Heme

Murata

Yoda

et al. 2011

The Journal of Veterinary Medical Science

Self Cite

View full text Add to dashboard Cite

ABSTRACT. The binding of ferritin to heme has been well studied using commercial horse spleen apoferritin, which is almost entirely composed of the L subunit, suggesting that mammalian ferritins bind heme. The present study revealed that both mammalian holoferritins (commercial horse spleen ferritin and purified horse spleen, bovine spleen and canine liver ferritins with L/H subunit ratios of 4.0, 1.1, and 2.3, respectively) and their apoferritins bound biotinylated hemin; apoferritins had higher binding activity than holoferritins, except for canine holo-and apoferritins, which showed the same binding. Bovine ferritin H subunit homopolymers expressed by a baculovirus expression system showed heme binding and had higher binding activity to biotinylated hemin than the L subunit homopolymer expressed by the same system. These bindings were inhibited by heme but not by iron-free or Zn-protoporphyrin IX (Zn-PPIX). Purified chicken liver holoferritin was found to be composed of only H subunits and showed the highest binding activity with biotinylated hemin compared with mammalian holoferritins. The binding of chicken liver holoferritin to biotinylated hemin was also inhibited by heme but not by PPIX or Zn-PPIX. These results indicate that mammalian and avian ferritins bind heme and that the H subunit preferentially recognizes heme.

show abstract

Section: Binding Of Mammalian Holo-and Apoferritins With Biotinylatedsupporting

confidence: 81%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Binding of Mammalian and Avian Ferritins with Biotinylated Hemin: Demonstration of Preferential Binding of the H Subunit to Heme

Murata

Yoda

et al. 2011

The Journal of Veterinary Medical Science

Self Cite

View full text Add to dashboard Cite

show abstract

“…The function of ferritins is to store a bioavailable and nontoxic form of iron to prevent its use in the production of highly toxic hydroxyl radicals through the iron-mediated Fenton reaction [3,5,14,16]. Mammalian ferritins are 24-mer proteins, composed of two types of subunits named the H (heart or heavy) and L (liver or light) subunits [1,5,15,20]. Chicken and bacterial ferritin subunits possess ferroxidase activity (iron-binding site) as in mammalian H subunits [1,3,7,13,23].…”

mentioning

confidence: 99%

Binding Analysis of Ferritin with Heme Using α-Casein and Biotinylated-Hemin: Detection of Heme-Binding Capacity of Dpr Derived from Heme Synthesis-Deficient <i>Streptococcus mutans</i>

Mieno

Yamamoto

Yoshikawa

et al. 2013

The Journal of Veterinary Medical Science

Self Cite

View full text Add to dashboard Cite

Mass spectrometric characteristics and kinetics of iron release in visceral mass of Saccostrea cucullata

Zhu

Huang

2011

Rapid Comm Mass Spectrometry

View full text Add to dashboard Cite

Ferritins with electrophoretic homogeneity were prepared from the visceral mass of Saccostrea cucullata in batch. The native PAGE approach showed similar electrophoretic mobility among pig pancreatic ferritin, liver ferritin of Dasyatis akajei, and visceral mass ferritin of Saccostrea cucullata. SDS-PAGE indicated that the Saccostrea cucullata visceral ferritin (SCVF) consisted of a single subunit type and had a molecular weight (MW) of approximately 20 kDa, suggesting that the protein shell in SCVF was composed of a single subunit. In addition, peptide mass fingerprinting and transmission electron microscopy were used to identify SCVF further, and to observe its molecular structure. We found that the molecular structure in SCVF was similar to that of most mammalian ferritins, which are composed of a protein shell and an iron core. The results of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry under the assistance of an acidic matrix, sinapic acid, also showed that SCVF was composed of a single subunit type and its subunit MW was calculated to be 19871.042 Da in the absence of heme. Kinetics analysis revealed that the complete process of iron release fitted the law of a first-order reaction, which is similar to that of most ferritins in mammals. Similar to bacterial ferritin, studies indicated that the shell consisted of a single subunit type and showed similar kinetics of iron release, suggesting that this subunit plays two important roles in iron release and storage, and that it shows different stability and intensity of interaction in carrying out its physiological functions in SCVF.

show abstract

Sequencing of cDNA Clones that Encode Bovine Ferritin H and L Chains

Cited by 36 publications

References 37 publications

Binding of Mammalian and Avian Ferritins with Biotinylated Hemin: Demonstration of Preferential Binding of the H Subunit to Heme

Binding of Mammalian and Avian Ferritins with Biotinylated Hemin: Demonstration of Preferential Binding of the H Subunit to Heme

Binding Analysis of Ferritin with Heme Using α-Casein and Biotinylated-Hemin: Detection of Heme-Binding Capacity of Dpr Derived from Heme Synthesis-Deficient <i>Streptococcus mutans</i>

Mass spectrometric characteristics and kinetics of iron release in visceral mass of Saccostrea cucullata

Contact Info

Product

Resources

About