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PubMed2006

Hydroxyalkylation of conjugated nitroalkenes with activated nonenolizable carbonyl compounds.

[reaction: see text] The Morita-Baylis-Hillman reaction of a variety of conjugated nitroalkenes with activated nonenolizable carbonyl compounds such as glyoxylate, trifluoropyruvate, pyruvaldehyde, and ninhydrin in the presence of 40-100 mol % of DMAP in acetonitrile or 100 mol % of imidazole in CHCl(3) or THF provided the adducts in decent to good yields. In most cases, the reactions catalyzed by DMAP in acetonitrile were faster and provided the desired MBH adducts in higher yields as compared to the imidazole catalyzed reactions.

Journal Article↗
PubMed1998

Bond cleavage reactions in solid aqueous carbohydrate solutions.

PURPOSE: To investigate chemical reactivity in water soluble glasses. METHODS: Rates of bond cleavage reactions in freeze-dried and freeze-concentrated aqueous carbohydrate solutions were measured above and below the glass transition temperatures (Tg). The kinetics of two reactions have been determined in formulations containing di- and polysaccharides: (1) fission of the Asp-Pro peptide bond in Physalaemin and Hamburger peptide by following the release of proline, using a ninhydrin based reaction and (2) the unimolecular dissociation of 2-(4-nitrophenoxy) tetrahydropyran by following the release of the 4-nitrophenoxy anion. RESULTS: The results show clearly that reaction occurs below the glass transition temperature, albeit at very reduced rates. No significant enhancement of the temperature dependence of the rate constant was observed near Tg. Different water soluble glasses provide different degrees of stability. The order of stabilisation was sucrose>Ficoll (low mol. weight)>Byco A approximately equal to Ficoll (high mol. weight)>dextran. The density of the matrix, and therefore the degrees of freedom of mobility of the reactant, is thought to be responsible for these differences. CONCLUSIONS: The storage of therapeutic agents, such as proteins, in glassy matrices below Tg does not confer indefinite stability. When formulating products, notice should be taken of the differing stabilisation properties of excipients.

Amino Acid Sequence↗
PubMed1976

Purification of a cytotoxic factor from human and rat tissues.

Human and rat normal tissues and tumours have been studied for the presence of toxic substances, possibly of importance in the development of cachexia in patients with cancer and other chronic diseases. The toxic effect of tissue extracts was gauged by measuring the inhibition of growth of mouse L-cells in 1-ml cultures, as revealed by reduced incorporation of [14C]leucine into cell protein. A common cytotoxic substance of mol. wt. approximately 700 daltons was isolated from all rat and human tissues tested, including tumours. The isolation procedure involved tissue homogenization, followed by pressure dialysis, gel filtration of concentrated pressure dialysates, cation exchange chromatography, and thin layer chromatography. Amounts isolated from different tissues varied by a factor of 3. The purified substance reacted with ninhydrin and a few other reagents for amino groups. It was completely resistant to acid and enzymatic hydrolysis. The evidence thus suggests that the substance is an amine. It is toxic to L-cells, HeLa cells and normal rat fibroblasts in concentrations of 10-20 muM, producing cell death and lysis during incubation overnight.

Animals↗
PubMed1994

Flow injection spectrophotometric determination of aspartame in dietary products.

A flow injection spectrophotometric method has been developed for the determination of aspartame in dietary products using ninhydrin as a colorimetric reagent. The reaction was conducted in a 1 + 1 v/v methanol-isopropanol medium also containing potassium hydroxide. The absorbance measurements were made at 603 nm. The results obtained for the determination of aspartame in table sweetener, pudding, gelatin, and refreshment (i.e., a powder dissolved in water for drinking) are in good agreement with the results obtained using a conventional manual procedure (correlation coefficient, r = 0.9984). Thirty-six results were obtained per hour, and the relative standard deviation was less than 3.5% (n = 6) for all samples. The detection limit (three times the signal blank/slope) was 3.8 x 10(-5) mol l-1 of aspartame.

Aspartame↗
PubMed1965

UPTAKE OF FREE PLASMA AMINO ACIDS BY THE LACTATING COW'S UDDER AND AMINO ACID COMPOSITION OF UDDER LYMPH.

1. Total alpha-amino N and the amounts of 24 ninhydrin-positive substances were determined in several samples of plasma and lymph from the cow's udder. The arteriovenous differences of these substances across the mammary glands were measured in several experiments performed on lactating cows and in one experiment on a ;dry' cow. Udder lymph obtained from live lactating cows by a lymph fistula and taken after killing lactating cows was analysed. 2. The concentrations of the individual free amino acids in udder lymph obtained from the live cow were similar to those found in cow's plasma. The concentrations of many amino acids in udder lymph taken immediately after death were two- to four-fold higher than those of the corresponding amino acids in udder lymph obtained from the live cow. 3. Most amino acids of the blood showed a considerable decrease in concentration by passage across the lactating mammary gland. Ornithine, a non-casein amino acid, showed arteriovenous differences of up to 60% of the arterial plasma concentration. No substantial amino acid uptake by the udder could be demonstrated in the experiment on the non-lactating cow. 4. The arteriovenous differences obtained for arginine, glutamine, isoleucine, leucine, lysine, valine, threonine and histidine were probably large enough to provide all the respective amino acid residues in milk protein. 5. The uptake of aspartic acid, asparagine, glutamic acid, serine and proline by the lactating cow's udder was not sufficient to account for all these respective amino acid residues found in milk protein.

Amino Acids↗
PubMed1965

STUDIES ON THE MUCIN DERIVED FROM HUMAN COLLOID BREAST CARCINOMA.

1. A non-diffusible mucoid, showing a single peak in the ultracentrifuge, was isolated from human colloid breast carcinoma by treatment with trypsin and pepsin. The material contained threonine, leucine (isoleucine), valine, proline, glycine and glutamic acid in the approximate molar proportions 5:1:1:2:1:1. Smaller amounts of aspartic acid and serine were also found. For each 5 threonine residues, 6 N-acetylgalactosamine and 3-4 galactose residues were present. 2. The mucoid possessed reducing properties by the Park & Johnson (1949) procedure; these were attributable to the action of mild alkali, as employed in this procedure. Mild alkaline treatment by the Aminoff, Morgan & Watkins (1952) procedure gave rise to a diffusible N-acetylgalactosamine chromophore that gave an enhanced colour with Ehrlich's reagent. That galactosyl-(1-->3)-N-acetylgalactosamine residues were liberated was supported by periodate studies. 3. Alkaline liberation of hexosamine residues was accompanied by a specific destruction of threonine. After 40 min. at 100 degrees in 0.18 n-lithium hydroxide, both moieties had almost completely disappeared from the ninhydrin-positive components formed on subsequent acid hydrolysis. Glycine and alpha-oxobutyric acid were present in the acid hydrolysate, showing that both possible pathways of a beta-elimination reaction were involved. Formation of diffusible peptide on very mild alkaline treatment was attributable to the rupture of the original peptide core, necessitated by the second of these two pathways. 4. Hydroxamate formation on treatment with hydroxylamine showed the presence of carbohydrate linkage to glutamic acid or aspartic acid residues or both. This could account for the single N-acetylgalactosamine residue not linked to threonine. 5. The native mucin contained sialic acid, which was cleaved by the acid environment used in the treatment with pepsin. A statistical model of the mucin would require each prosthetic group to be linked, via N-acetylgalactosamine, to threonine, which would occupy every alternate position among the amino acids in the peptide core.

Adenocarcinoma, Mucinous↗
PubMed1965

FURTHER OBSERVATIONS ON THE PRODUCTION OF AMINO ACIDS BY RAT-LIVER MITOCHONDRIA AND OTHER SUBCELLULAR FRACTIONS.

1. Rat-liver mitochondria showed a decrease in amino acid production after preparation in 0.25m-sucrose containing EDTA (1mm), but an increase in water content. When EDTA was replaced by Mn(2+) (1mm) or succinate (1mm), both amino acid production and water content were lowered, whereas preparation in 0.9% potassium chloride caused an increase in both. 2. Amino acid production by rat-liver homogenates prepared in 0.9% potassium chloride or 0.25m-sucrose was similar (q(amino acid) 0.047 and 0.042 respectively aerobically). After freezing-and-thawing q(amino acid) values were approximately doubled, and approached that of a homogenate prepared in water. 3. All cations tested inhibited amino acid production by mitochondria, Hg(2+) and Zn(2+) being the most effective in tris-hydrochloric acid buffer. In phosphate buffer Mg(2+) and Mn(2+) had no effect. Of the anions tested only pyrophosphate and arsenate had any inhibitory effect at final concn. 1mm. 4. Iodosobenzoate (1mm) and p-chloromercuribenzenesulphonate (1mm) inhibited mitochondrial amino acid production by 70-80%, whereas soya-bean trypsin inhibitor, EDTA and di-isopropyl phosphorofluoridate inhibited by a maximum of 30%. Respiratory inhibitors had no effect. 5. Rat-liver homogenate and subcellular fractions each showed an individual pattern of inhibition when a series of inhibitors was tested. 6. Amino acid production by mitochondria was decreased by up to 50% in the presence of oxidizable substrate, apart from alpha-glycerophosphate and palmitate, which had no effect. CoA stimulated amino acid production in tris-hydrochloric acid but not in phosphate buffer, alpha-oxoglutarate abolishing the stimulation. 7. Cysteine and glutathione stimulated amino acid production by whole mitochondria by 30%, but only reduced glutathione stimulated production in broken mitochondria. 8. Adrenocorticotrophic hormone and growth hormone stimulated mitochondrial amino acid production by 21-24%, whereas insulin inhibited production by 25%. 9. Coupled oxidative phosphorylation increased amino acid production by up to 154% at 25 degrees and 40 degrees . The increase was abolished by 2,4-dinitrophenol. 10. Amino acid incorporation in mitochondria was accompanied by an increase in amino acid production, both being decreased by chloramphenicol. 11. Mitochondrial production of ninhydrin-positive material was increased in the presence of albumin. The biggest increase was noted for the soluble fraction of broken mitochondria. No increase was found in the presence of (14)C-labelled algal protein or denatured mitochondrial protein.

Amino Acids↗
PubMed1965

Accumulation of amino acids in muscle of perfused rat heart. Effect of insulin in the presence of puromycin.

1. Rat heart was perfused with a mixture of amino acids and other ninhydrin-positive substances in the same concentrations as they are found in plasma, and with or without sufficient puromycin to suppress protein synthesis all but completely. 2. In the presence of puromycin, but not in its absence, insulin increased the concentrations of most of the individual amino acids in the intracellular water of heart. 3. The results accord with the conclusion that insulin increases the entry of most, if not all, amino acids into muscle.

Journal Article↗
PubMed1965

Production and purification of bacilysin.

1. Bacilysin, a hydrophilic substance formed by certain aerobic spore-forming bacteria that causes lysis in cultures of growing staphylococci, has been produced in aerated cultures of a strain of Bacillus subtilis (A14). A chemically defined medium was used, which contained glucose, Czapek-Dox salts and ferric iron. Production of bacilysin occurred, after a lag, while the culture was still undergoing rapid growth. 2. Bacilysin was adsorbed from the culture medium on Zeo-Karb 225 (SR5) (H(+) form) and eluted with aqueous pyridine. The crude material was purified by chromatography in pyridine-acetate buffers on columns of Dowex 50 (X2) and Dowex 50 (X8) respectively and by chromatography in aq. 70% (v/v) propan-2-ol on Sephadex G-25. 3. Purified bacilysin behaved as a single ninhydrin-positive substance when subjected to chromatography on paper in butan-1-ol-acetic acid-water and to electrophoresis on paper at pH4.5 or pH1.8. At pH4.5 the substance behaved as though it had no net change and at pH1.8 it migrated towards the cathode.

Journal Article↗
PubMed1966

The isolation and partial characterization of glycolipids of normal human leucocytes.

1. The lipids of purified human leucocytes were extracted with chloroform-methanol and the extract was washed with water. Glycolipids, isolated by Florisil chromatography, were subjected to mild alkaline hydrolysis and the alkali-resistant fraction was fractionated on a silicic acid column. 2. Three classes of glycolipid were separated. The less polar, containing 3.6% of the total glycolipid hexose as galactose, was tentatively identified as ceramide monohexoside. The major glycolipid fraction was characterized as ceramide dihexosides. The more polar glycolipids comprised 1.6% of the total glycolipid hexose as galactose and glucose (in the molar ratio 2:1) and were non-acidic. This class was separated as a mixture containing ninhydrin-positive glycolipids. 3. The ceramide dihexosides taken from two leucocyte preparations accounted for 15.2% and 16.4% by weight of the total lipids. 4. The carbohydrate moiety of the ceramide dihexosides contained galactose and glucose in the molar ratio 2:1. Partial acid hydrolysis and paper chromatography indicated that the hexoses are present as disaccharides, lactose being identified as one of them. 5. Palmitic acid (C(16:0)) and nervonic acid (C(24:1)) were the major fatty acids of this glycolipid. Hydroxy fatty acids were not detected.

Chemical Phenomena↗
PubMed1967

Esters of serine and threonine in hydrolysates of histones and protamines, and attendant errors in amino acid analyses of proteins.

1. Partial acid hydrolysates of histones from various origins and of protamine were analysed by a two-dimensional ionophoretic procedure to reveal strongly acidic ninhydrin-positive components. 2. Histone fractions prepared by extraction with sulphuric acid gave rise to spots identified as serine O-sulphate and threonine O-sulphate. These two compounds, which were not found in hydrolysates of corresponding fractions prepared by extraction with hydrochloric acid, were artifacts. 3. Hydrolysis of proteins in the presence of traces of sulphate can lead to the formation of the O-sulphates of serine and threonine. This can cause errors, which may sometimes be serious, in amino acid analyses of proteins. 4. O-Phosphoserine was obtained in small amounts from some histone fractions and from protamine, but was undetectable in other histone fractions, notably those of lower lysine content.

Activation Analysis↗
PubMed1967

The aminoethylphosphonate-containing lipids of rumen protozoa.

1. A method is presented for identifying and estimating the aminoethylphosphonate (ciliatine)-containing phospholipids in a complex mixture. 2. Evidence was obtained that the phospholipids of a pure culture of Entodinium caudatum and a mixed rumen protozoa sample contain diglyceride ciliatine, and a plasmalogen ciliatine was detected in the latter. 3. A ninhydrin-positive sphingolipid was isolated from rumen protozoa. Although chromatographically homogeneous on silica gel it contains two components, which were provisionally identified as ceramide ciliatine and ceramide phosphorylethanolamine. 4. A detailed phospholipid analysis of E. caudatum and rumen protozoa is presented. They contain no phosphatidylserine or cardiolipin, but an unidentified phosphoglyceride containing a zwitterionic amino acid is present.

Animals↗
PubMed1968

Structural changes in mitochondria induced by uncoupling reagents. The response to proteolytic enzymes.

Interaction of uncoupling reagents with bovine serum albumin markedly inhibited its hydrolysis by proteolytic enzymes. The inhibition presumably is due to conformational transitions in the protein substrate induced by the binding of the ligand-uncoupling reagents. The proteolysis of casein, a protein that does not bind these reagents, was not affected, indicating that the proteinases themselves were not inactivated. In contrast, interaction of uncoupling reagents with freshly isolated rat liver mitochondria enhanced their susceptibility to proteolytic enzymes. This was shown by an increase in the release of ninhydrin-reacting material, by an increase in free acid groups and by a decrease in the turbidity of the mitochondrial suspensions. These effects, although opposite in direction to those obtained with albumin, are also presumed to indicate structural changes in the mitochondrial proteins and a disorganization of the protein-phospholipid complex. It is suggested that such structural alterations are expressed functionally as the uncoupling of oxidative phosphorylation.

Amobarbital↗
PubMed1968

N-Terminal acetyl-peptides from two calf thymus histones.

1. The same N-terminal peptide was isolated from two major calf thymus histone fractions, F2al and F2a2. 2. The structure of the peptides is N-acetylseryl-glycyl-arginine, and the yields account for most of the N-acetyl groups previously found in these histones. 3. Some other peptides not giving a ninhydrin reaction were also investigated.

Animals↗
PubMed1969

The pH-dependence of pepsin-catalysed reactions.

1. The pH-dependence of the pepsin-catalysed hydrolysis of three peptide substrates was studied by using a method for the continuous monitoring of the formation of ninhydrin-positive products. 2. Two peptide acid substrates, N-acetyl-l-phenylalanyl-l-phenylalanine and N-acetyl-l-phenylalanyl-l-phenylalanyl-glycine, show apparent pK(a) values of 1.1 and 3.5 in the plots of k(0)/K(m) versus pH. By contrast a neutral substrate, N-acetyl-l-phenylalanyl-l-phenylalanine amide, shows apparent pK(a) values of 1.0 and 4.7. 3. Together with the data of the preceding paper (Knowles, Sharp & Greenwell, 1969), these results are taken to indicate that the rate of pepsin-catalysed hydrolysis is controlled by the ionization of two groups, which on the free enzyme have apparent pK(a) values of 1.0 and 4.7. It is apparent that the anions of peptide acid substrates are not perceptibly bound to the enzyme, resulting in apparent pK(a) values of 3.5 for the dependence of k(0)/K(m) for these materials.

Amides↗
PubMed1969

Beta-alanyl-L-tyrosine. Chemical synthesis, properties and occurrence in larvae of the fleshfly Sarcophaga bullata Parker.

1. A naturally occurring peptide, termed sarcophagine, has been isolated from larvae of the fleshfly Sarcophaga bullata. 2. The physicochemical properties of the natural peptide are identical with those of synthetic beta-alanyl-l-tyrosine. 3. During larval growth the concentration of the dipeptide increases continuously; in the fully grown larva it is the predominant non-protein ninhydrin-positive material. 4. Sarcophagine is rapidly and extensively utilized at the time of hardening and darkening of the insect puparium. 5. By virtue of its much higher solubility than that of free tyrosine, the peptide may serve as a reservoir to provide large amounts of readily available tyrosine for subsequent puparium formation.

Alanine↗
PubMed1970

Degradation of insulin by a particulate fraction from adipose tissue.

The destruction of (125)I-labelled insulin by an enzyme system from rat adipose tissue was studied. The system was located in the particulate fraction. Activity was assayed by the amount of (125)I-labelled degradation products rendered soluble in trichloroacetic acid. The system was heat-labile, with an alkaline pH optimum. The velocity of the reaction varied directly with the enzyme concentration. Paper chromatography of the degradation products showed six ninhydrin-sensitive areas with radioactivity coinciding with three of them. Albumin inhibited the system; ribonuclease did not. Although only 25% of the total (125)I-label was detected by this assay, results with insulin-specific assays suggested that most (80-90%) of the hormone was inactivated. Possible interpretations of these results are discussed. The particulate fractions of other tissues were also studied.

Adipose Tissue↗
PubMed1970

Mescaline-induced changes of brain-cortex ribosomes. Effect of mescaline on the stability of brain-cortex ribosomes.

1. During the action of mescaline sulphate on goat brain-cortex slices the ribosomal particles become susceptible to breakdown, releasing protein, RNA, acidsoluble nucleotides and ninhydrin-positive materials, resulting in loss of ribosomal enzyme activities. 2. Ribosomes of the mescaline-treated cortex slices undergo rapid degradation in the presence of trypsin and ribonuclease. 3. Mescaline does not alter the chemical and nucleotide compositions or the u.v.-absorption characteristics of ribosomal particles, however.

Animals↗