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Opioid Peptides from Milk Proteins
The human β-casein amide, Tyr-Pro-Phe-Val-NH2 (valmuceptin) was the most active, more than the bovine counterpart, morphiceptin, and was named β-casorphin and α-lactorphin, respectively.
Purification and Characterization of an Opioid Antagonist from a Peptic Digest of Bovine κ-Casein
A chloroform/methanol extract of a peptic digest of bovine K-casein had binding activity to opioid receptors of rat brain and was an antagonist selective for the μ- and κ-types of opioid receptors.
Characterization of a dinuclear MnV=O complex and is efficient evolution of O2 in the presence of water.
Opioid antagonist peptides derived from κ-casein
Summary Opioid antagonists were sought in the fragments of κ-casein which were obtained by chemical synthesis and enzymic digestion. A synthetic bovine κ-casein peptide (35–41),…
Characterization of β-Lactotensin, a Bioactive Peptide Derived from Bovine β-Lactoglobulin, as a Neurotensin Agonist
- Rena Yamauchi, H. Usui, J. Yunden, Y. Takenaka, F. Tani, M. Yoshikawa
- Biology, Chemistry
- 1 January 2003
The results suggest that the hypertensive activity of β-LT is mediated by the NT2 receptor, and it was concluded that the NT1 and NT2 receptors mediate the opposite effect on blood pressure.
Heat-induced Transparent Gel Formation of Bovine Serum Albumin.
- M. Murata, F. Tani, T. Higasa, N. Kitabatake, E. Doi
- Materials ScienceBioscience, biotechnology, and biochemistry
- 23 January 1993
The formation of transparent gels by 6% bovine serum albumin (BSA), pH 7.5, was examined by one- and two-step heating methods and the mechanism of transparent gel formation in BSA may be similar to that in ovalbumin.
Isolation and characterization of opioid antagonist peptides derived from human lactoferrin.
- F. Tani, K. Iio, H. Chiba, M. Yoshikawa
- Biology, ChemistryAgricultural and biological chemistry
- 1 July 1990
A study of the structure-activity relationship of the three lactoferroxins and their synthetic analogues showed that these opioid antagonist peptides derived from food protein could be expressed by the general formula XA-Tyr-XB-T Tyr-OCH3.
Five amino acid residues in cysteine-rich domain of human T1R3 were involved in the response for sweet-tasting protein, thaumatin.
One-electron oxidized nickel(II)-(disalicylidene)diamine complex: temperature-dependent tautomerism between Ni(III)-phenolate and Ni(II)-phenoxyl radical states.
- Y. Shimazaki, F. Tani, Kôichi Fukui, Y. Naruta, O. Yamauchi
- Chemistry, PhysicsJournal of the American Chemical Society
- 7 August 2003
The one-electron oxidized species of a Ni(II)-phenolate complex has been shown to be in the Ni(II)-phenoxyl radical state at room temperature and the Ni(III)-phenolate state at < -120 degrees C,…