Chemical modification of arginine by nitromalondialdehyde. Synthesis and properties of δ-(5-nitro-2-pyrimidyl)ornithyl derivatives

Signor, A.; Bonora, Gian Maria; Biondi, Laura; Nisato, Dino; Marzotto, A.; Scoffone, Ernesto

doi:10.1021/bi00790a015

Cited by 26 publications

(11 citation statements)

References 22 publications

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“…• C for 2 h. Upon cooling and acidification, a mixture of diphenyl disulfide [26] and 3,5-dinitro-2-pyridone [27] was obtained and separated by fractional crystallization [22]. The same procedure was repeated for all the title solvents that gave the same results.…”

Section: Experimental Materialsmentioning

confidence: 99%

Solvent effect on the alkaline hydrolysis of 2‐thiophenyl‐ 3,5‐dinitropyridine

Fathalla¹

2006

Int J of Chemical Kinetics

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The kinetics of the alkaline hydrolysis of 2-thiophenyl-3,5-dinitropyridine were studied spectrophotometrically in different aquo-organic solvents such as methanol, ethanol, npropyl alcohol, iso-propyl alcohol, t-butyl alcohol, acetonitrile, dimethyl sulfoxide, dioxane, and acetone at 30 • C with various solvent compositions up to 80% (v/v) of organic components. An increase in the organic solvent percentage (v/v) has different effects on the reaction rate constants presumably due to hydrogen bond donor HBD and acceptor HBA of the medium and other solvatochromic parameters. Linear and nonlinear plots of log k against the reciprocal of the dielectric constant of the solvent were obtained. The effects are too complex to be analyzed in terms of a single parameter, but an approach using the Kamlet-Taft solvatochromic parameters is applied successfully to six mixed aquo-organic solvent systems. C 2006 Wiley Periodicals, Inc. Int J Chem Kinet 38: 159-165, 2006

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Section: Experimental Materialsmentioning

confidence: 99%

Solvent effect on the alkaline hydrolysis of 2‐thiophenyl‐ 3,5‐dinitropyridine

Fathalla¹

2006

Int J of Chemical Kinetics

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“…After tryptic digestion a peptide map was made and two ultraviolet-absorbing spots (at 366 nm) were visible before staining with ninhydrin. After elution and hydrolysis of these spots, one gives the amino acid composition of T,, plus T,, and the other that of T,, plus T,, with the expection that ornithine was found instead of arginine [36].…”

Section: Peptide Ch (Positions 79-94)mentioning

confidence: 99%

The Primary Structure of an Acidic Protein from 50‐S Ribosomes of Escherichia coli which is Involved in GTP Hydrolysis Dependent on Elongation Factors G and T

Terhorst¹,

Möller²,

Laursen

et al. 1973

European Journal of Biochemistry

206

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The primary structures of the ribosomal proteins A, (= L,) and A, (= L,,) have been elucidated. Comparison of the two amino acid sequences confirms earlier studies by us (1972) which indicated that the two proteins are identical except that A, possesses an N-terminal acetyl group.Sequencing of tryptic and chymotryptic peptides was accomplished primarily by automatic solid-phase Edman degradation of 50-to 70-nanomole peptide samples. A large tryptic peptide T,Phe, which could not be sequenced by this method, was fragmented with elastase and its sequence mainly derived by conventional methods. The sequence of the first 51 residues of the nonacetylated A,-protein was obtained by Edman degradation in the Beckman sequencer.A-protein comprises three distinct regions : I (residues 1 -55), which is negatively-charged and hydrophobic, I1 (56-81), which is positively charged, and I11 (82-120), which is negatively charged and hydrophilic. &-Helix promoting residues are located primarily in regions I and 111. e-N-Monomethyllysine, which occurs in 50°/, of the A, and A, chains is located in the more flexible region I1 at position 81.The distinctive clustering of hydrophobic and charged residues is quite remarkable and suggests that in situ certain of these regions may contain a binding site for components involved in peptide chain elongation.

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“…The bovine basic protein was reacted with nitromalonyl dialdehyde by the method of Signor et al [7] as previously described for the human basic protein [8]. The resulting/5-(5-nitro-2-pyrimidyl) ornithine derivative of the basic protein (NP-A1) was reduced with sodium borohydride to the 1,4,5,6,-tetrahydropyrimidyl derivative (THP-A1) [7].…”

Section: Methodsmentioning

confidence: 99%

“…The resulting/5-(5-nitro-2-pyrimidyl) ornithine derivative of the basic protein (NP-A1) was reduced with sodium borohydride to the 1,4,5,6,-tetrahydropyrimidyl derivative (THP-A1) [7]. NP-A1 (10 mg) was suspended in 0.8 ml absolute ethanol; 0.2 ml of 0.1 N NaOH was added followed by 10 mg sodium borohydride which was added as a dry powder with stirring.…”

Section: Methodsmentioning

confidence: 99%