Effect of bromide salts on the acid hydrolysis of anti-bacterial hydrophilic Schiff base amino acid iron(II) complexes

2014 ◽  
Vol 84 (10) ◽  
pp. 2037-2042 ◽  
Author(s):  
Ali M. Shaker ◽  
Lobna A. E. Nassr ◽  
Mohamed S. S. Adam ◽  
Ibrahim M. A. Mohamed
Keyword(s):  
Schiff Base ◽  
Amino Acid ◽  
Acid Hydrolysis ◽  
Hydrolysis Of

A kinetic study of the acid autoxidation of tryptophan

1972 ◽  
Vol 25 (10) ◽  
pp. 2139 ◽  
Author(s):  
M Stewart ◽  
CH Nicholls
Keyword(s):  
Free Radical ◽  
Amino Acid ◽  
Kinetic Study ◽  
Acid Hydrolysis ◽  
Soda Glass ◽  
Glass Containers ◽  
Hydrolysis Of

The decomposition of tryptophan in aqueous HC1 at 100�C has been shown to proceed by a free-radical autoxidation mechanism. The acid functions by protonating the amino acid at either the 1- or 3-positions prior to autoxidation and so 1-methyltryptophan is also decomposed under these conditions. Impurities present in the soda glass containers used are shown to be responsible for the initiation of the reaction. The decomposition of tryptophan during the acid hydrolysis of proteins is considered in the light of these results.

Correction for Amino Acid Loss during Acid Hydrolysis of a Purified Protein

1996 ◽  
Vol 236 (2) ◽  
pp. 199-207 ◽  
Author(s):  
Alison J. Darragh ◽  
Dorian J. Garrick ◽  
Paul J. Moughan ◽  
Wouter H. Hendriks
Keyword(s):  
Amino Acid ◽  
Acid Hydrolysis ◽  
Hydrolysis Of

Hydrophilicity and acid hydrolysis of water-soluble antibacterial iron(II) Schiff base complexes in binary aqueous solvents

2013 ◽  
Vol 83 (12) ◽  
pp. 2460-2464 ◽  
Author(s):  
Ali M. Shaker ◽  
Lobna A. E. Nassr ◽  
Mohamed S. S. Adam ◽  
Ibrahim M. A. Mohamed
Keyword(s):  
Schiff Base ◽  
Acid Hydrolysis ◽  
Water Soluble ◽  
Schiff Base Complexes ◽  
Hydrolysis Of

D-Mannitol Interferes with Amino Acid Analysis of Marine Organisms

1979 ◽  
Vol 36 (9) ◽  
pp. 1134-1137 ◽  
Author(s):  
W. Fong ◽  
R. K. O'dor
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Hydrolysis ◽  
Key Words ◽  
Amino Acid Analysis ◽  
Chromatographic Analysis ◽  
Marine Algae ◽  
Protein S ◽  
New Compounds ◽  
Hydrolysis Of

Acid hydrolysis of a protein in the presence of D-mannitol, a common constituent of marine algae, can cause significant reductions in the recovery of a number of amino acids. The new compounds formed by the interactions of D-mannitol and these amino acids may interfere in the chromatographic analysis of other amino acids. The recoveries of most of the amino acids appear to be either directly or inversely proportional to the amount of D-mannitol added to a protein sample before acid hydrolysis. These results suggest that it is necessary to determine the effects of contaminants in a sample of protein(s) on the recoveries of amino acids during routine acid hydrolysis. Key words: kelp, amino acids, carbohydrates, D-mannitol

ACTION OF PROTEOLYTIC ENZYMES ON SOIL ORGANIC MATTER

1970 ◽  
Vol 50 (2) ◽  
pp. 233-241 ◽  
Author(s):  
F. J. SOWDEN
Keyword(s):  
Amino Acids ◽  
Organic Matter ◽  
Amino Acid ◽  
Soil Organic Matter ◽  
Acid Hydrolysis ◽  
Leucine Aminopeptidase ◽  
Proteolytic Enzymes ◽  
Complexing Agent ◽  
Organic Matter Fractions ◽  
Hydrolysis Of

The amino acids set free by proteolytic enzymes were determined with an amino acid analyzer. Soil and enzyme blanks were subtracted. Pronase released 2 to 10% of the aspartic acid + asparagine, threonine, serine, glutamic acid + glutamine, glycine, lysine and histidine in some fractions of soil organic matter along with 15–35% of the alanine, valine, isoleucine, leucine, tyrosine, phenylalanine and arginine. There was no release of proline, ornithine or ammonia. When the pronase hydrolysate was treated with leucine amino-peptidase, 15% of the proline was released, the yield of glycine was raised from 2 to 14% and the amount of the acidic amino acids was also higher. Acid hydrolysis of the pronase hydrolysate also released more amino acid material but the blanks were much higher than with leucine aminopeptidase. The results suggested that more than half of the aspartic and glutamic acids found on acid hydrolysis were present in the soil organic matter fractions as asparagine and glutamine. The action of pronase on the organic matter of the intact soil was slight, even in the presence of a complexing agent. Papain released very little amino acid material from organic matter fractions, but leucine aminopeptidase or HCl hydrolysis of the papain hydrolysate released about 10% of the amino acid of the fraction, indicating that significant amounts of peptides were formed on papain treatment.

scholarly journals The hydrolysis of proteins by microwave energy

1991 ◽  
Vol 13 (3) ◽  
pp. 93-95 ◽  
Author(s):  
Sam A. Margolis ◽  
Lois Jassie ◽  
H. M. Kingston
Keyword(s):  
Amino Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Acid Hydrolysis ◽  
Bovine Serum ◽  
Microwave Energy ◽  
Complete Hydrolysis ◽  
Hydrolysis Conditions ◽  
Hydrolysis Of

Microwave energy, at manually-adjusted, partial power settings has been used to hydrolyse bovine serum albumin at 125 °C. Hydrolysis was complete within 2 h, except for valine and isoleucine which were completely liberated within 4 h. The aminoacid destruction was less than that observed at similar hydrolysis conditions with other methods and complete hydrolysis was achieved more rapidly. These results provide a basis for automating the process of amino-acid hydrolysis.

scholarly journals Studies on Reduced Wool VI. Comparison of Peptides Containing S-Carboxymethylcysteinyl Residues in Different Protein Fractions

1965 ◽  
Vol 18 (6) ◽  
pp. 1227 ◽  
Author(s):  
IJ O'donnell ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Acid Hydrolysis ◽  
Aromatic Amino Acid ◽  
Protein Fractions ◽  
Cysteine Residues ◽  
Partial Acid Hydrolysis ◽  
Chromatographic Methods ◽  
Hydrolysis Of ◽  
Peptide Maps

Wool has been reduced and extracted by urea-mercaptoethanol solution and the cysteine residues labelled by carboxymethylation with 2-[14C]iodoacetate. The extracted protein has been fractionated into the three main classes of protein present in wool, namely the high-sulphur, low-sulphur, and high-glycine-high-aromatic amino acid fractions. After partial acid hydrolysis of each fraction, peptide maps were prepared by paper ionophoretic and chromatographic methods and the S-carboxymethyl- containing peptides located by radioautography. The peptide maps given by the three fractions were almost identical in the peptides obtained, although marked differences in intensities were apparent. However, radioautographs of peptide maps of tryptic digests of the three fractions showed marked differences in the peptide patterns obtained. The findings are discussed in relation to the structure and synthesis of wool.

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