Bay: the Noncombatant as War Poet

Cushman, Keith

doi:10.1007/978-1-349-06510-3_12

Cited by 8 publications

(9 citation statements)

References 1 publication

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“…With respect to the inhibitory activity against ACE, [19] desferri-tsukubachelin showed the most potent inhibitory activity, with an IC50 value of 1.4 μg/mL. For structureactivity comparison, the IC50 value of authentic desferriforoxymithine was also determined to be 20.1 μg/mL in the same experiment.…”

Section: Resultsmentioning

confidence: 97%

“…The extraction of total DNA from the cells of TM-34 was performed according to the previous paper. [19] The 16S rRNA-encoding sequence was amplified from the total DNA by PCR using two universal primer pairs: 9F (5Ј-GAGTTTGATCCTGGCTCAG-3Ј) and 1541R (5Ј-CTCCTACGGGTGAGTAACAC-3Ј). The reaction mixture for PCR was prepared by adding 0.5 μL of total DNA of TM-34 (100 ng), 0.5 μL of LA taq DNA polymerase (Takara, Japan), 25 μL of X2 GC buffer (Takara, Japan), 4 μL of 2.5 mm dNTPmix solution (Takara, Japan), and 20 μL of distilled water into the PCR reaction tube.…”

Section: Polymerase Chain Reaction (Pcr) Amplification Sequencing Amentioning

confidence: 99%

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A New Siderophore Isolated from Streptomyces sp. TM‐34 with Potent Inhibitory Activity Against Angiotensin‐Converting Enzyme

Kodani¹,

Ohnishi‐Kameyama

Yoshida

et al. 2011

Eur J Org Chem

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A new siderophore named tsukubachelin was isolated from an iron-deficient culture medium of newly isolated strain Streptomyces sp. TM-34. The chemical structure of tsukubachelin was established by the interpretation of 2D NMR and TOF-Mass spectroscopic data. The structure of tsukubachelin consists of six amino acid residues, including three serine, and one each of N-α-methyl-N-δ-hydroxy-N-δ-formylornithine, N-α-methyl-N-δ-hydroxyornithine, and cyclic Nhydroxyornithine. Because the structurally related sidero-

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Section: Resultsmentioning

confidence: 97%

Section: Polymerase Chain Reaction (Pcr) Amplification Sequencing Amentioning

confidence: 99%

A New Siderophore Isolated from Streptomyces sp. TM‐34 with Potent Inhibitory Activity Against Angiotensin‐Converting Enzyme

Kodani¹,

Ohnishi‐Kameyama

Yoshida

et al. 2011

Eur J Org Chem

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“…These peptides were assayed in vitro for the ability to inhibit ACE activity according to the method of the National Food Research Institute (Tsukuba city, Japan) with some modifications as mentioned in a previous report. 17 In brief, 100 mL of 4.7 mM hippuryl-L-histidyl-L-leucine/300 mM NaCl/400 mM phosphate buffer solution (pH 8.5) was added with 50 mL of testing peptide or vehicle used to dissolve the testing peptide. Then, 100 mL (2.5 mU) of ACE/ distilled water was mixed with the above substrate solution to initiate the reaction that was carried out by incubation in a water bath at 37 ± 1°C under shaking for 60 min.…”

Section: Measurement Of Ace Inhibitionmentioning

confidence: 99%

Essential of Proline and Valine Residues in the Peptide Derived from Lactoferrin for Angiotensin Converting Enzyme Inhibition

Lee

Cheng

Enomoto

et al. 2006

Jnl Chinese Chemical Soc

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We synthesized Leu‐Arg‐Pro‐Val‐Ala‐Ala‐Glu, the peptide contained in lactoferrin (Lf), to identify the angiotensin converting enzyme (ACE) inhibition. In an attempt to know the structure‐activity relationship of this peptide, we replaced Pro (the third amino acid residues from N‐terminal) or Val (the fourth amino acid residues from N‐terminal) with Ala (neutral amino acid), Glu (acidic amino acid) or Lys (basic amino acid) to produce six peptides. From the in vitro ACE inhibition (IC50) of these synthesized peptides, the original peptide (Leu‐Arg‐Pro‐Val‐Ala‐Ala‐Glu) showed higher ACE inhibition than the replaced six peptides. Thus, replacement of Pro at the third amino acid residues or Val at the fourth position with Ala, Glu or Lys revealed the ACE inhibition to be lower than the original form of Leu‐Arg‐Pro‐Val‐Ala‐Ala‐Glu. Otherwise, we added one peptide at the C‐terminal of Leu‐Arg‐Pro‐Val‐Ala‐Ala‐Glu and found both products with an addition of Val (Leu‐Arg‐Pro‐Val‐Ala‐Ala‐Glu‐Val) or Ile (Leu‐Arg‐Pro‐Val‐Ala‐Ala‐Glu‐Ile) showing a lower ACE inhibition than the original one. The ACE inhibitions produced by both replaced peptides were without significance. Also, deletion of the last peptide at the C‐terminal (Leu‐Arg‐Pro‐Val‐Ala‐Ala) failed to produce a marked change of ACE inhibition as compared to the original one. These results suggest that Pro and Val are essential in the peptide for inhibition of ACE activity.

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“…The supernatant was filtered (0.45 µm pore size). Then the ACE-inhibition activity of the filtrate was measured according to Cushman and Cheung [9] with some modification. Briefly, 200 µl of HHL buffer (5 mM Hip-His-Leu in 0.1 M borate buffer containing 0.3 M NaCl, pH 8.3) was mixed with 60 µl of borate buffer and pre-incubated with 20 µl of inhibitory solution for 5 min at 37 mC.…”

Section: Enzyme Activity Assaymentioning

confidence: 99%

Yeast protease B‐digested skimmed milk inhibits angiotensin‐I‐converting‐enzyme activity

Roy

Watanabe

Tamai

2000

Biotech and App Biochem

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Angiotensin-1-converting-enzyme (ACE) inhibitory activity was identified in skimmed milk digested with cell-free extract of yeast Saccharomyces cerevisiae. Simultaneously, a protease enzyme involved in the production of ACE-inhibition materials in digested skimmed milk was purified to homogeneity from the cell-free extracts of S. cerevisiae by ammonium sulphate fractionation and chromatography in DEAE-Sephacel, D-tryptophan methyl ester-Sepharose 4B, Hiload Superdex G-200 and HPLC Mono-Q chromatography. The purified enzyme was identified as protease B, based on the molecular mass on SDS/PAGE and the N-terminal amino acid sequence of the enzyme. The optimum pH for digestion of skimmed milk and production of ACE-inhibition materials was pH 4.8. The IC(50) of the hydrolysate was 0.42 mg of protein/ml when skimmed milk was digested with yeast protease B.

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Bay: the Noncombatant as War Poet

Cited by 8 publications

References 1 publication

A New Siderophore Isolated from Streptomyces sp. TM‐34 with Potent Inhibitory Activity Against Angiotensin‐Converting Enzyme

A New Siderophore Isolated from Streptomyces sp. TM‐34 with Potent Inhibitory Activity Against Angiotensin‐Converting Enzyme

Essential of Proline and Valine Residues in the Peptide Derived from Lactoferrin for Angiotensin Converting Enzyme Inhibition

Yeast protease B‐digested skimmed milk inhibits angiotensin‐I‐converting‐enzyme activity

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