A contribution to the chemistry of proteids

Hopkins, Frederick Gowland; Cole, Sydney W.

doi:10.1113/jphysiol.1901.sp000880

Cited by 166 publications

(14 citation statements)

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“…This observation led to the naming of tryptophan as the as-yet-unidentified source of indole in proteins by Neumeister in 1890 [6]. Tryptophan was first isolated from casein by Hopkins and Cole in 1901 [7], followed by the demonstration that tryptophan was in fact the source of indole formed by bacteria in 1903 [8]. Indole formation from tryptophan is a characteristic property of enteric bacteria, especially Escherichia coli, which inhabit the gut of animals [9].…”

Section: Introductionmentioning

confidence: 99%

The role of substrate strain in the mechanism of the carbon–carbon lyases

Phillips¹,

Demidkina²,

Faleev³

2014

Bioorganic Chemistry

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Section: Introductionmentioning

confidence: 99%

The role of substrate strain in the mechanism of the carbon–carbon lyases

Phillips¹,

Demidkina²,

Faleev³

2014

Bioorganic Chemistry

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“…The name "tryptophan" (W, molecular formula: C 11 H 12 N 2 O 2 , molecular mass: 204.23 Da) originates from the time when this 20 amino acid was first isolated from a casein (CN) tryptic digest by Hopkins and Cole 1 . Of the twenty conventional amino acids, W is the only one which possesses an indole structure.…”

Section: Introductionmentioning

confidence: 99%

Milk proteins as a source of tryptophan-containing bioactive peptides

Nongonierma

Fitzgerald

2015

Food Funct.

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Tryptophan (W) is an essential amino acid which is primarily required for protein synthesis. It also acts as 5 a precursor of key biomolecules for human health (serotonin, melatonin, tryptamine, niacin, nicotinamide adenine dinucleotide (NAD), phosphorylated NAD (NADP), quinolinic acid, kynureric acid, etc.). Among dietary proteins, milk proteins are particularly rich in W. W residues within milk proteins may be released by proteolytic/peptidolytic enzymes either as a free amino acid or as part of peptide sequences. Different W-containing peptides originating from milk proteins have been shown in vitro to display a 10 wide range of bioactivities such as angiotensin converting enzyme (ACE) inhibition along with antioxidant, antidiabetic and satiating related properties. Free W has been shown in certain instances to have an effect on cognition and the aforementioned bioactive properties. However, a higher bioactive potency has generally been observed with specific W-containing peptides compared to free W. Since W is thermolabile, the impact of processing on the stability of W-containing peptides needs to be considered. 15Milk protein-derived W-containing peptides may have significant potential as natural health promoting agents in humans.

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“…The distinguishing structural characteristic of tryptophan is that it contains an indole functional group. The isolation of tryptophan was first reported by Hopkins in 1901 through hydrolysis of casein [3].…”

Section: Introductionmentioning

confidence: 99%

Spectrophotometric investigation of DL-tryptophan in the presence of Ni(II) or Co(II) ions

Altun

Bilcen

2012

Eur. J. Chem.

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KEYWORDSIn the present study, synthesis of transition metal complexes of DL-tryptophan with metal precursors such as nickel (II) and cobalt (II) ions in water under refluxing conditions and optimization of the reactions to obtain the composition of complexes in water solutions has been reported. The preparation and structural elucidation of the complexes was undertaken by using physico-chemical, potentiometric titration and spectroscopic methods (UV/Vis, FT-IR and XRD). Comparisons of the spectral measurements of DL-tryptophan with those of the nickel (II) and cobalt (II) complexes are useful in determining the atoms of the ligand that are coordinated to the metal ion. In addition, K (dissociation constant) and ΔG (Gibbs free energy) values were calculated using the Babko and Stanley & Turners methods. Antibacterial and antifungal activities of the complexes were studied screened against bacteria and fungi. The activity data shows that and cobalt complexes of DL-tryptophan are more potent than the DLtryptophan.

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A contribution to the chemistry of proteids

Cited by 166 publications

References 0 publications

The role of substrate strain in the mechanism of the carbon–carbon lyases

The role of substrate strain in the mechanism of the carbon–carbon lyases

Milk proteins as a source of tryptophan-containing bioactive peptides

Spectrophotometric investigation of DL-tryptophan in the presence of Ni(II) or Co(II) ions

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