Amino Acid Analysis Using Pre-Column Derivatization with Phenylisothiocyanate: Matrix Effects and Tryptophan Analysis

Cohen, Steven A.; Tarvin, Thomas L.; Bidlingmeyer, Brian A.

doi:10.1007/978-1-4613-1787-6_22

Cited by 11 publications

(6 citation statements)

References 7 publications

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“…AsnMe at position p72 could be identified by amino acid sequencing and amino acid analysis by pre-column derivatisation with phenylisothiocyanate. For this purpose, the derivatisation procedure of Cohen et al (1987) was slightly modified in order to detect the methylamine moiety released by the hydrolysis of AsnMe (Rumbeli et al, 1987). As expected, the hydrolysis of the pure p5S-p77 fragment released a single aspartic acid residue together with the methylamine moiety originating from the hydrolysed AsnMe (Fig.…”

Section: The Complete Amino Acid Sequence Of R-phycocyanin-i From F! mentioning

confidence: 93%

“…Rapid amino acid analysis from peptides purified by two-dimensional HPLC and from carboxypeptidase Y degradation experiments was performed by the pre-column derivatisation method with phenylisothiocyanate according to Heinrickson and Meredith (1984). The free amino acids were derivatised according to the method of Cohen et al (1987). The detection of the methylamine arising from the hydrolysis of y-N-methyl asparagine was achieved by allowing the free amino acids to react without further manipulation with phenylisothiocyanate.…”

Section: Hydrolysis and Amino Acid Analysismentioning

confidence: 99%

See 1 more Smart Citation

The complete amino acid sequence of R‐phycocyanin‐I α and β subunits from the red alga Porphyridium cruentum

Ducret¹,

Sidler²,

Frank³

et al. 1994

European Journal of Biochemistry

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We present here the complete primary structure of R-phycocyanin-I a and p subunits from the red alga Porphyridium cruentum. The a chain is composed of 162 amino acid residues (18049Da, calculated from sequence, including chromophore) and carries a phycocyanobilin pigment covalently linked to Cys84. The p chain contains 172 amino acids (19344Da, calculated from sequence, including chromophores) and carries a phycocyanobilin pigment covalently linked at Cys82 and a phycoerythrobilin pigment at Cys153. A y-N-methyl asparagine residue was also characterised at position ,872 similar to other phycobiliprotein , 6 subunits. R-phycocyanin-I from Porphyridium cruentum shares high sequence identity with C-phycocyanins (69 -83%), R-phycocyanins (66-70%) and in a less extent with phycoerythrocyanins (57-65%) from various sources.The presented phylogenetic trees are based on a comparison of all phycobiliprotein amino acid sequences known so far and confirm the clear affiliation of the R-phycocyanins in the phycocyanin family. In spite of their particular phycobilin pattern, they do not represent intermediate forms between the phycocyanin and the phycoerythrin family. Phycoerythrocyanin, a phycocyanin-related phycobiliprotein adapted to green light harvesting, is also shown to belong to the phycocyanin family. However, the phycoerythrocyanins diverge from phycocyanins in their different function and it is suggested that they should be assigned to a separate group within the phycocyanin family.Phycobilisomes represent the main accessory light-harvesting antenna of cyanobacteria and red algae (Cohen-Bazire and Bryant, 1982;Zuber, 1983Glazer, 1984Glazer, , 1985Gantt, 1988;Bryant, 1991; Sidler, 1994). Their major components, the phycobiliproteins, are constituted of a and p subunits (16-18 kDa and 18-20 kDa respectively) carrying one, two or three open-chain tetrapyrroles (bilins) per subunit as prosthetic groups. Both subunits are aggregated in vivo to heterotrimers (an3 or hexamers (anb. Electron microscopy and crystal structure analysis show that the trimer complex is the basic building block of the phycobilisome (Schirmer et al., 1985). The ap monomer aggregates in a disc-shaped complex with a diameter of 11 nm and a length of 3 nm. A hexamer is built up of two trimers stacked face-to-face (Schirmer et al., 1986). The formation of higher aggregatesCorrespondence to H.

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Section: The Complete Amino Acid Sequence Of R-phycocyanin-i From F! mentioning

confidence: 93%

Section: Hydrolysis and Amino Acid Analysismentioning

confidence: 99%

The complete amino acid sequence of R‐phycocyanin‐I α and β subunits from the red alga Porphyridium cruentum

Ducret¹,

Sidler²,

Frank³

et al. 1994

European Journal of Biochemistry

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“…Cysteine and methionine were analyzed after performic acid oxidation and determined as cysteic acid and methionine sulfone, respectively. Tryptophan was hydrolyzed with methanosulfonic acid [21].…”

Section: Diet Preparation and Analysismentioning

confidence: 99%

Protein nutritional quality of cowpea and navy bean residue fractions

Jackson¹

2009

African Journal of Food, Agriculture, Nutrition and Development

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Cereal-legume protein complementation has long been recommended as a suitable strategy for augmenting the protein quality of cereal and legume based foods. However, the use of the insoluble legume residue, following protein extraction for cereal-legume protein complementation has not been widely studied. In fact, legume residue is considered a waste by-product. The protein quality of cowpea residuewheat and navy bean residue-wheat diets was determined using in-vivo and in-vitro protein digestibility assays with an AIN-93G diet as control. The diets were fed to laboratory rats over 4 weeks. The in-vitro digestibility of the diets was assessed using the pH drop and pH stat enzymatic methods. The proximate composition, limiting amino acid profile and phytohemagglutinin activity were also determined. All six diets had lower levels of the sulphur amino acid requirements for rats as expected but had higher than the FAO/WHO recommended levels for preschool children. The cowpea residue diets had higher levels of limiting amino acids than the navy bean residue diets. Phytohemagglutinin activity was only detectable in the raw cowpea and navy bean samples. All cowpea residue diets, the 30% and 70% navy bean residue diets and the control diet supported growth while the 100% navy bean residue diet resulted in weight loss. The in-vitro digestibility ranged from 77.82%-84.54% and 66.51%-79.59% for the cowpea residue and the navy bean residue diets, respectively. These ranges were lower than the control (98.1%) but correlated highly to those obtained using the in-vivo true protein digestibility method; 73.7%-87.5% and 62.6%-78.2%, respectively. These findings suggest that the cowpea residue diets had higher protein quality overall than the navy bean residue diets. In addition, it suggests that the 30:70 ratio of cowpea residue to wheat diet had the highest protein quality of all the 6 experimental diets. Legume residues after protein extraction could be recommended for human food if complemented with a cereal, particularly as it meets the amino acid pattern for preschool children. Finally, in-vitro assays can also be reliably used to assess the protein quality of foods.

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“…Gross energy was measured in an isoperibolic bomb calorimeter (Parr Instrument Co., Moline, IL, USA). AA composition of diets (Alanine (Ala), Aspartic acid (Asp), Cysteine (Cys), Glutamic acid (Glu), Glycine (Gly), Histidine (His), Isoleucine (Iso), Leucine (Leu), Lysine (Lys), Methionine (Met), Phenylalanine (Phe), Proline (Pro), Serine (Ser), Threonine (Thr), Tyrosine (Tyr), and Valine (Val)) was determined after protein hydrolysis in 6 mol/L hydrochloric acid plus 10 g/kg phenol in sealed tubes at 110 °C for 24 h, by high performance liquid chromatography (HPLC) using the Waters Pico-Tag method for hydrolysates which involves pre-column with phenylisothiocyanate [ 16 ] and a Waters Nova-Pak C18 phase reverse column (4 µm, 3.9 × 150 mm). Cys and Met in the diet were determined as cysteic acid and Met sulphone, respectively, obtained by oxidation with performic acid before protein hydrolysis [ 17 ].…”

Section: Methodsmentioning

confidence: 99%

Net Portal Appearance of Amino Acids in Iberian and Landrace Pigs Fed Different Protein Content in the Diet

Lachica

Rodríguez-López

González-Valero

et al. 2023

Animals

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Iberian pigs have low rates of muscle protein deposition compared with modern breeds. Differences in net portal appearance (NPA) of amino acids (AA) might partially explain that. NPA of AA was measured in six Iberian and six Landrace gilts (28 kg) fitted with catheters in portal and mesenteric (para-aminohippuric acid infusion) veins, and carotid artery. Blood samples from porta and artery were simultaneously taken at 0, 0.5, 1, 1.5, 2, 2.5, 3, 3.5, 4, 5, and 6-h after feeding two isoenergetic diets (14–14.5 MJ metabolizable energy/kg dry matter) with different crude protein (145 (LCP) and 187 (HCP) g/kg dry matter) content. NPA of essential AA (EAA) and non-essential AA (NEAA) was lower (p < 0.05) in Iberian than Landrace pigs, and in LCP than HCP diet. Fractional absorption (NPA/AA intake) of EAA, NEAA, and total AA was, respectively, 36, 49, and 44% lower in LCP than HCP diet in Iberian pigs; and 8, 2, and 4% greater in Landrace pigs. Fractional absorption of EAA, NEAA, and total AA was 42, 68, and 60% lower in Iberian than Landrace pigs fed LPC diet; and 1, 36, and 26% when fed the HCP diet. NPA of AA may partially explain the low growth rate of Iberian pigs.

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Amino Acid Analysis Using Pre-Column Derivatization with Phenylisothiocyanate: Matrix Effects and Tryptophan Analysis

Cited by 11 publications

References 7 publications

The complete amino acid sequence of R‐phycocyanin‐I α and β subunits from the red alga Porphyridium cruentum

The complete amino acid sequence of R‐phycocyanin‐I α and β subunits from the red alga Porphyridium cruentum

Protein nutritional quality of cowpea and navy bean residue fractions

Net Portal Appearance of Amino Acids in Iberian and Landrace Pigs Fed Different Protein Content in the Diet

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