Measurement of Tryptophan in Peptides by Acid Hydrolysis in the Presence of Phenol and its Application to the Amino Acid Sequence of a Sea Anemone Toxin

Muramoto, Koji; Sunahara, Satoshi; Kamiya, Hisao

doi:10.1080/00021369.1987.10868227

Cited by 3 publications

(3 citation statements)

References 6 publications

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“…The amino acid composition of the STC and the fragment peptides was determined using an automated amino acid analyzer (Hitachi, Model L-8500, Tokyo) after hydrolysis with 6 M HCI containing 0.6% phenol at 110°C (Muramoto et al, 1987).…”

Section: Amino Acid Sequence Analysismentioning

confidence: 99%

Effects of a synthetic N-terminal fragment of stanniocalcin on the metabolism of mammalian bone in vitro

Yoshiko

Kosugi

Koide

1996

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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A synthetic peptide corresponding to the N-terminal amino acid residues of stanniocalcin (STC1-20) and including a region that is known to be an active site in teleosts was prepared and tested for its effects on the metabolism of mammalian bone in vitro. STC1-20 (10(-10)-10(-12) M) inhibited increases in the number of tartrate-resistant acid phosphatase-positive, multinucleated cells promoted by an N-terminal fragment of human parathyroid hormone (hPTH1-34) in cultures of murine hemopoietic cells. STC1-20 also slightly decreased the rate of loss of radioactivity from calvariae of fetal rats that had been prelabeled with 45Ca, both with and without stimulation by hPTH1-34. The accumulation of cAMP induced by hPTH1-34 in ROS 17/2.8-5 cells was suppressed by STC1-20 (10(-10)-10(-12) M). Treatment with STC1-20 (10(-11)-10(-13) M) caused increases of the rate of incorporation of [3H]proline into the collagenase-digestible protein of calvariae in newborn mice. From these results, it appears that STC1-20 has diverse effects on the metabolism of mammalian bone, causing a biphasic response. Such effects have not been observed with intact stanniocalcin or with materials from the corpuscles of Stannius and they are also different from the effects of hPTH1-34.

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Section: Amino Acid Sequence Analysismentioning

confidence: 99%

Effects of a synthetic N-terminal fragment of stanniocalcin on the metabolism of mammalian bone in vitro

Yoshiko

Kosugi

Koide

1996

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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“…Determination of the total amino acid composition of samples was determined using hydrolysis with 6 M HCl at 110 °C for 23 h, [ 34 ]. The samples were then deproteinized by mixing equal volumes of 24% ( w / v ) tri-chloroacetic acid and sample.…”

Section: Methodsmentioning

confidence: 99%

Angiotensin-I-Converting Enzyme Inhibitory Activity of Protein Hydrolysates Generated from the Macroalga Laminaria digitata (Hudson) JV Lamouroux 1813

Purcell

Packer

Hayes

2022

Foods

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Seaweeds have a long history of use as both food and medicine, especially in Asian cultures. Moreover, there is growing interest in the use of seaweed ingredients and bioactive compounds in pharmaceutical and nutraceutical products. One ailment that seaweed bioactive compounds may impact is hypertension caused by the enzyme Angiotensin Converting Enzyme 1 (ACE-1; EC 3.4.15.1), found within the Renin-Angiotensin Aldosterone System (RAAS), which causes vasoconstriction of blood vessels, including veins and arteries. The aim of this paper is to generate bioactive peptide containing protein hydrolysates from the brown seaweed Laminaria digitata (Hudson) JV Lamouroux 1813. Proteins were extracted from this seaweed by disrupting the seaweed cell wall using a combination of carbohydrases and proteolytic enzymes. Bioactive peptide containing permeates were generated from L. digitata protein hydrolysates, and both hydrolysates and permeates were screened for their ability to inhibit the enzyme ACE-1. The protein content of the permeate fractions was found to be 23.87% compared to the untreated seaweed, which contained 15.08% protein using LECO analysis. Hydrolysis and filtration resulted in a “white” protein powder, and the protein content of this powder increased by 9% compared to the whole seaweed. The total amino acid (TAA) content of the L. digitata protein permeate was 53.65 g/100 g of the sample, and contains over 32% essential amino acids (EAA). Furthermore, the L. digitata permeate was found to inhibit the ACE-1 enzyme by 75% when compared to the commercial drug Captopril© when assayed at a concentration of 1 mg/mL. The inhibition of ACE-1 (the IC50 value) of 590 µg/mL for the L. digitata permeate compares well with Captopril©, which had 100% inhibition of ACE-1, with an IC50 value of 500 µg/mL. This study indicates that there is potential to develop protein powders with ACE-1 inhibitory bioactivities from the brown seaweed L. digitata using enzymatic hydrolysis as a cell disruption and protein extraction/hydrolysate generation procedure.

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“…Confirmation of molecular weights of the pentafluoropropionamide isopropyl ester derivatives was obtained by chemical ionization mass spectrometry with isobutane as the reagent gas. In attempts to detect tryptophan, acid hydrolyses were also conducted in the presence of 1% phenol (10).…”

Section: Methodsmentioning

confidence: 99%

Insecticidal Components from Field Pea Extracts: Isolation and Separation of Peptide Mixtures Related to Pea Albumin 1b

Taylor

Fields

Elder

2004

J. Agric. Food Chem.

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Chromatographic fractionation of crude extracts (C8 extracts) from the protein-enriched flour of commercial field peas (Pisum sativum L.) has been shown here to yield peptide mixtures related to the pea albumin 1b (PA1b) family of cysteine-rich plant peptides. The mixtures were obtained initially by flash chromatography with silica gel. Following elution of soyasaponins and lysolecithins, the end fractions obtained with the use of two flash chromatographic solvent systems displayed activity in a flour disk antifeedant bioassay with the rice weevil [Sitophilus oryzae (L.)]. Chemical properties of these mixtures were compared by thin-layer chromatography, high-performance liquid chromatography (HPLC), IR, MS, and amino acid analyses. The major peptides of C8 extracts, with average masses of 3752, 3757, and 3805 Da, were isolated by anion exchange chromatography. Samples enriched in the peptide of mass 3752 were isolated by cation exchange chromatography. Reduction plus alkylation experiments in combination with electrospray ionization mass spectrometry showed that C8 extracts contained about 10 peptides and, like PA1b, each peptide possessed six cysteine residues (three disulfide bonds). Disulfide bond reduction with 2-mercaptoethanol destroyed the antifeedant activity. The native peptides of C8 extracts were found to be resolved into nine peaks with XTerra HPLC columns operating at alkaline pH. These columns were employed to assess the distribution of pea peptides in the isolated fractions, with photodiode array and electrospray detection.

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Measurement of Tryptophan in Peptides by Acid Hydrolysis in the Presence of Phenol and its Application to the Amino Acid Sequence of a Sea Anemone Toxin

Cited by 3 publications

References 6 publications

Effects of a synthetic N-terminal fragment of stanniocalcin on the metabolism of mammalian bone in vitro

Effects of a synthetic N-terminal fragment of stanniocalcin on the metabolism of mammalian bone in vitro

Angiotensin-I-Converting Enzyme Inhibitory Activity of Protein Hydrolysates Generated from the Macroalga Laminaria digitata (Hudson) JV Lamouroux 1813

Insecticidal Components from Field Pea Extracts: Isolation and Separation of Peptide Mixtures Related to Pea Albumin 1b

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