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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ferritin from the soyabean Glycine max was isolated and characterized. The protein has many features in common with ferritin from mammalian systems, including extensive sequence homology, as determined by two-dimensional peptide mapping. No immunocross-reactivity between the plant and animal proteins was detected. The ferritin isolated by MgCl2 precipitation has a single subunit of 28 kDa, whereas the ferritin remaining in the supernatant exhibits marked heterogeneity, with a main subunit of 22 kDa. This form of the protein appears to be the result of specific proteolytic processing that is not affected by serine protease inhibitors, and appears only after the seeds have been soaked long enough to induce germination. The appearance of the 22-kDa form corresponds to the appearance of "crystalline arrays" of ferritin in the amyloplasts of the plant cotyledons and may represent a plant form of hemosiderin. In support of this hypothesis, the 22-kDa protein appears to be incompletely assembled, as determined by sucrose gradient centrifugation and iron uptake studies. Although ferritin is normally quite resistant to proteolysis, the 22-kDa protein is easily generated from the 28-kDa form by treatment with subtilisin, suggesting the presence of a specific, protease-sensitive sequence on the protein's surface, possibly used to mark the phytoferritin for conversion to hemosiderin and construction of ferritin crystalline arrays.
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PMID:Isolation and characterization of ferritin from soyabeans (Glycine max). 365 37

Antioxidant peptides are increasingly being recognized as food additives due to their effects on body human, regulating in vivo oxidative stress against oxidation of lipids and proteins. Meat by-products are rich sources of protein that can be employed for this purpose. Specifically, porcine liver can be used to prepare hydrolysates with antioxidant activity employing proteolytic enzymes such as alcalase, bromelain, papain and flavourzyme. In this study, the antioxidant activity of these four porcine liver hydrolysates was evaluated by 2,2-diphenyl-1-picrylhydrazyl (DPPH), ((2,2-azinobis-(3-ethyl-benzothiazoline-6-sulphonate) (ABTS), Ferric reducing antioxidant power assay (FRAP) and Oxygen radical absorbance capacity assay (ORAC) assays and the identification of bioactive peptides was carried out by SWATH-MS technology. According to the SDS-PAGE pattern, the proteolysis index and the free amino acids amount, the protein degradation was clearly different among the studied enzymes. Indeed, alcalase enzyme produced the release of small peptides, meanwhile flavourzyme produced higher level of free amino acids. The heatmap analysis showed a peptidomic pattern more differentiated for alcalase than for the other enzymes. The peptides most abundant and correlated with antioxidant capacity were APAAIGPYSQAVLVDR from uncharacterized protein, GLNQALVDLHALGSAR, ALFQDVQKPSQDEWGK and LSGPQAGLGEYLFER from ferritin and LGEHNIDVLEGNEQFINAAK from trypsinogen. The production and characterization of biopeptides is a new merging challenge of meat industry.
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PMID:Antioxidant activity and peptidomic analysis of porcine liver hydrolysates using alcalase, bromelain, flavourzyme and papain enzymes. 3323 91