2001
DOI: 10.1271/bbb.65.736
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Designing Potent Derivatives of Ovokinin(2-7), an Anti-hypertensive Peptide Derived from Ovalbumin

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Cited by 50 publications
(29 citation statements)
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“…Anyhow, it seems that no general strategy for improving bioavailability of antihypertensive peptides exists and due to the number of processes involved and different characteristics of peptides depending on the sequence each case must be studied. Many strategies are currently demonstrated for enhancing bioavailability [171], among them microencapsulation for controlled release of the active compounds, stabilization of the active molecules to improve transportation through the intestinal barrier and provide resistance against degradation, and development of highly stabile peptide analogues [172][173][174].…”
Section: Bioavailabilitymentioning
confidence: 99%
See 1 more Smart Citation
“…Anyhow, it seems that no general strategy for improving bioavailability of antihypertensive peptides exists and due to the number of processes involved and different characteristics of peptides depending on the sequence each case must be studied. Many strategies are currently demonstrated for enhancing bioavailability [171], among them microencapsulation for controlled release of the active compounds, stabilization of the active molecules to improve transportation through the intestinal barrier and provide resistance against degradation, and development of highly stabile peptide analogues [172][173][174].…”
Section: Bioavailabilitymentioning
confidence: 99%
“…in the regulation of blood pressure and circulation, and these receptors are related to the antihypertensive properties of some food derived peptides. Other vasodilatory substances, such as ET-1, have also been suggested to be involved in the antihypertensive effects of food-derived peptides [173,178,179]. However, peptide sequences derived specifically from plant proteins inducing endothelial NO liberation have not been reported this far.…”
Section: Health Benefitsmentioning
confidence: 99%
“…This subunit was expressed in E. coli, recovered from the soluble fraction and purified by chromatography. The Arg-Pro-Leu-Lys-Pro-Trp peptide was released from recombinant containing subunit after digestion by trypsin and chymotrypsin [52]. Feeney et al [53] reported that the construction of glutenin genes and their expression in E.coli is a viable method for producing peptides.…”
Section: Pepsinmentioning
confidence: 99%
“…Its vasorelaxing activity was mediated by the B1 receptor. On the other hand, Ovokinin(2-7) (RADHPF) was isolated from a trypsin digest of ovalbumin based on vasorelaxing activity in mesenteric artery isolated from SHR [52]. It showed a weak affinity for the AT2 receptor.…”
Section: C) Egg Proteinsmentioning
confidence: 99%