1.Tetrapod-type [Asp1] angiotensin is present in a holostean fish, Amia calva.
Takei Y1, Itahara Y, Butler DG, Watanabe TX, Oudit GY. Gen Comp Endocrinol. 1998 May;110(2):140-6.
The renin-angiotensin system has been identified in various vertebrates, from elasmobranchs to mammals. Tetrapod (amphibians to mammals) angiotensin (ANG) has Asp at the N-terminus, but Asp is replaced by Asn in elasmobranch and teleost fish. ANG I has been isolated from incubates of plasma and kidney extracts of the bowfin Amia calva, a holostean fish, using the eel vasopressor activity as an assay system; its sequence was found to be H-Asp-Arg-Val-Tyr-Val-His-Pro-Phe-Asn-Leu-OH after sequence analysis, mass spectrometry, and comparison with the synthetic peptide. This sequence is identical to bullfrog ANG I. [Asn1] ANG I was not detected. Thus the bowfin is the first fish species which contains only [Asp1] ANG I. The bowfin ANG I and II were no more vasopressor than eel peptides in the bowfin, indicating that bowfin ANG II receptors do not distinguish between [Asp1] and [Asn1] peptides. In the rat, bowfin ANG I and rat [Ile5, His9] ANG I have equipressor activities when examined in different animals, but the vasopressor activity of bowfin ANG I decreased following rat ANG I in the same animals, although the activity of rat ANG I was unaffected after bowfin ANG I.
2.Vasopressor and depressor effects of native angiotensins and inhibition of these effects in the Japanese quail.
Takei Y1, Hasegawa Y. Gen Comp Endocrinol. 1990 Jul;79(1):12-22.
The amino acid sequence of angiotensin I (ANG I) from the Japanese quail, Coturnix coturnix japonica, obtained from incubation of homologous plasma and kidney extract was determined as H-Asp-Arg-Val-Tyr-Val-His-Pro-Phe-Ser-Leu-OH. A bolus, intravenous injection of native ANG I or of ANG II induced an immediate vasodepressor response and a subsequent vasopressor response in quail which has been lightly anesthetized with urethane (0.75 g/kg). The values for ED50 for the vasopressor and depressor effects of ANG II were 85 and 113 pmol/100 g body weight, respectively. The extent of the hypotension was dependent on the arterial pressure prior to injection. The effects of ANG I and II on heart rate were variable. Human [Asp1, Ile5, His9] ANG I and II were almost as potent as their quail counterparts with respect to the cardiovascular effects, but eel [Asn1, Val5, Gly9]ANG I and II were less than half as potent. Human ANG III had little effect on arterial pressure in the quail.
3.Lack of tuberculin activity of synthetic peptides.
Toida I, Yamamoto S, Takuma S, Suzuki T, Hirata M. Infect Immun. 1985 Dec;50(3):614-9.
We synthesized an octapeptide, H-Asp-Gly-Gly-Ser-Glu-Ser-Glu-Gly-OH, and a hexadecapeptide, H-Asp-Gly-Gly-Ser-Glu-Ser-Glu-Gly-Lys-Asn-Gly-Ser-Gln-Met-Arg-Leu-OH, which corresponded to amino acids 61 to 68 and 61 to 76, respectively, of the amino acid sequence of a crystalline protein reported to be tuberculin active. Authenticity and purity of the synthesized peptides were confirmed by high-pressure liquid chromatography, amino acid analysis, mass spectrometry, and protein sequencer analysis. Tuberculin activity of the synthesized peptides was examined in guinea pigs sensitized with Mycobacterium tuberculosis or Mycobacterium bovis BCG and in tuberculin-positive healthy humans. Neither the octa- nor the hexadecapeptide was as active as tuberculin skin-test antigen.
4.[Selective recognition and detection of biomacromolecules utilizing chemical property of amino Acid or Peptide].
Umezawa N1, Akita S, Kamoto M, Higuchi T. Yakugaku Zasshi. 2007 Dec;127(12):1915-25.
Recently, the fluorometric detection of biomacromolecules has attracted much attention. In this paper, we report the development of two new techniques utilizing the chemical properties of amino acids or peptides: 1) a fluorescence assay for serine/threonine kinase activity; and 2) "turn-on" fluorescent probes for protein labeling, which could be useful for bioimaging. To develop the novel kinase assay, we utilized the chemical reactivity of phosphorylated serine or threonine. Phosphorylated peptide on resin was successfully labeled fluorescently via base-mediated beta-elimination, followed by Michael addition with novel coumarin derivatives. Protein kinase A and casein kinase I activities were detectable with our method. Also, this method was confirmed to be applicable for kinase inhibitor screening. For the development of the novel protein labeling technique, the selective interaction between "His-tag (His(6))" and "metal ion nitrilotriacetic acid (NTA) complex" was utilized.
