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PubMed2001

Chemical Modifications on Human Hair Studied by Means of Contact Angle Determination.

Wetting properties of a solid surface can change as a consequence of chemical treatment. There is a relationship between the molecular structure of a surface and the macroscopic properties of this surface such as wetting and adhesion. Information on the surface energy of a solid was obtained by calculating polar and dispersion force contributions by means of contact angle determination. The superficial modification undergone by human hair treatments with or without hydrogen peroxide at alkaline pH was studied by means of wetting force measurements. The wetting increase in treated human hair fibers was analyzed following the Hüttinger method using contact angle data, taking into account the acid-base and dispersion components of the total wetting adhesion work. The hydrogen peroxide treatment at alkaline pH leads to a partial removal of hydrocarbon chains and to the formation of ionic groups (cysteic acid residues) on the outer scale cell surface. The latter phenomenon was observed by means of an increase in the acid-base adhesion work versus water wetting liquid at alkaline pH. Copyright 2001 Academic Press.

Journal Article↗
PubMed1986

Studies on the methods for the determination of phosphorylation sites in highly phosphorylated peptides or proteins: phosphorylation sites of hen egg white riboflavin binding protein.

To determine the phosphate binding sites in hen egg white riboflavin binding protein (RBP), a highly phosphorylated peptide, which consisted of 23 amino acid residues including eight phosphoserines, was isolated from the tryptic digest of reduced and carboxymethylated RBP. The conditions of the beta-elimination-addition reaction to convert phosphoserine residues in the peptide to cysteic acids, S-methylcysteines, alanines, and beta-methylaminoalanines (DL-alpha-amino-beta-methylamino propionic acid) were examined. These converted peptides were purified by HPLC and subjected to Edman degradation. The results of Edman degradation indicated that the S-methylcysteine derivative of the peptide gave the most satisfactory result for determining the phosphate binding sites in the peptide. The phosphorylation sites of the peptide determined by the method mentioned above are as follows: His182-Leu-Leu-Ser185-Glu-Ser(P)-Ser(P)-Glu-Glu190-Ser (P)-Ser(P)-Ser(P)-Met-Ser195(P)-Ser(P)-Ser(P)-Glu-Glu-. These studies indicated that the conversion of phosphoserines in phosphoproteins to S-methylcysteines followed by Edman analysis was a useful method for the elucidation of the phosphorylation sites in phosphopeptides.

Amino Acid Sequence↗
PubMed2001

A novel tandem quadrupole mass spectrometer allowing gaseous collisional activation and surface induced dissociation.

A novel tandem quadrupole mass spectrometer is described that enables gaseous collision-induced dissociation (CID) and surface-induced dissociation (SID) experiments. The instrument consists of a commercially available triple quadrupole mass spectrometer connected to an SID region and an additional, orthogonal quadrupole mass analyser. The performance of the instrument was evaluated using leucine-enkephalin, allowing a comparison between CID and SID, and with previous reports of other SID instruments. The reproducibility of SID data was assessed by replicate determinations of the collision energy required for 50% dissociation of leucine-enkephalin; excellent precision was observed (standard deviation of 0.6 eV) though, unexpectedly, the reproducibility of the equivalent figure for CID was superior. Several peptides were analysed using SID in conjunction with liquid secondary-ion mass spectrometry or electrospray; a comparison of the fragmentation of singly protonated peptide ions and the further dissociation of y-type fragments was consistent with the equivalence of the latter fragments to protonated peptides. Few product ions attributable to high-energy cleavages of amino acid side-chains were observed. The SID properties were investigated of a series of peptides differing only in the derivatization of a cysteine residue; similar decomposition efficiencies were observed for all except the cysteic acid analogue, which demonstrated significantly more facile fragmentation.

Amino Acid Sequence↗
PubMed1986

Sex differences in blood amino acid concentration and cell/plasma distribution in the domestic fowl.

The amino acid concentration of and distribution between the cell and plasma of the blood of male and non-laying female domestic fowl have been determined. No significant differences in plasma amino acid content were observed between the sexes, except for higher serine and lower asparagine concentrations in the female. Hens had higher intracellular concentrations of aspartate, hydroxyproline, arginine, lysine and cystine and lower concentrations of cysteic acid and taurine. The proportion of amino acids carried in the blood cells of fowls was about 80%, a value that is much higher than that found in mammals. The mean ratio of combined total amino acid concentrations between plasma and cells was about 8-fold, again much higher than the corresponding figures in mammals.

Amino Acids↗
PubMed1979

Chromatographic analysis of hydroxylysine glycosides and acid hydrolyzates.

A single-column chromatographic technique for the analysis of hydroxylysine glycosides and acid hydrolyzates is described. This technique employs a Durrum D-500 amino acid analyzer equipped with a standard 48 cm X 1.8 mm column packed with DC-4A resin. Resolution was achieved with four sodium citrate buffers and four column temperatures. Products of glycoprotein hydrolysis including cysteic acid, methionine sulfoxide, 4-hydroxyproline, alpha-aminobutyric acid, glucosamine, galactosamine, hydroxylysine, tryptophan and the internal standard, norleucine, are resolved. The completely automated procedure takes 185 min per run and can measure amino acid residues in the nanomole range.

Animals↗
PubMed1988

Oxidation of amino acids and peptides in reaction with myeloperoxidase, chloride and hydrogen peroxide.

Oxidation was studied of N-acetyl derivatives of cystine, cysteine, methionine and glycyltryptophan employing the myeloperoxidase-Cl--H2O2 system at pH 4.5, 6.0 and 7.0. Moreover, oxidation of pentapeptide composed of Leu-Trp-Met-Arg-Phe-COOH with myeloperoxidase (donor:hydrogen-peroxide oxidoreductase, EC 1.11.1.7) and hypochlorite was also studied. It was found that amino-acid derivatives having an amino group bound to an acetyl residue react with functional groups of the side-chain. The -SH groups of N-acetylcysteine and the -SS- group of cystine oxidize to cysteic acid. Methionine residues oxidize to methionine sulphoxide, and tryptophan residues to a derivative of 2-oxoindolone. The same reaction products were obtained when respective amounts of hypochlorous acid were used instead of myeloperoxidase, Cl- and H2O2. Differences in the stoichiometry of reactions of myeloperoxidase-mediated oxidation and hypochlorite oxidation suggest differences in the reaction mechanisms of both studied systems. Interaction of the studied pentapeptide with myeloperoxidase-Cl(-)-H2O2 system as well as with hypochlorite showed that in the peptide molecule individual amino acids oxidize consecutively according to their susceptibility to oxidation. No splitting of peptide bonds was observed. Therefore, a modified peptide with methionine sulphoxide and and oxidized tryptophan incorporated into the molecule was obtained.

Amino Acids↗
PubMed1976

The effects of selenium on the metabolism of methionine in sheep.

Two groups of sheep fed a diet of hay known to produce nutritional muscular dystrophy, one group of which received selenium supplementation, were used to study the effects of selenium on the metabolism of administered L-(35S) methionine by rumen microflora. Rumen bacterial proteins of the Se supplemented sheep contained significantly higher levels of radiosulfur than the bacterial protein of the non-supplemented sheep. Of hte L-(35S) methionine present in the rumen liquor samples from Se-supplemented sheep 2 h after administration, 13.3% of the amino acid, which was measured as methionine sulfone, was found in the microbial proteins. A large proportion of the administered labeled methionine was resynthesized as cyst(e)ine which may account in part for that determined as cysteic acid in rumen bacterial and plasma proteins. The observed low levels of radiosulfur found in rumen microflora from selenium deficient wethers, indicates that the presence of selenium profoundly affects the rate of methionine metabolism and the distribution of methionine in rumen bacterial and protozoal proteins. In another experiment, the effect of selenium on the metabolism of L-(Me-3H) methionine was studied. The selenium status of the sheep had no significant effect (P greater than 0.05) on the distribution of 35S radioactivity in the blood plasma and tissues.

Amino Acids↗
PubMed1968

Transport of aminophosphonic acids in Lactobacillus plantarum and Streptococcus faecalis.

Aminophosphonic acids analogous to glutamic acid, aspartic acid, alanine, and valine were actively accumulated by Lactobacillus plantarum. Uptake was dependent on the availability of glucose and, in all cases, the estimated intracellular concentrations substantially exceeded extracellular levels. During uptake, there was little metabolism of tritiated 2-amino-3-phosphonopropionic acid (APP), the aspartic acid analogue, and a negligible incorporation of isotope from this substance into the nucleic acid, lipid, protein, or cell wall fractions of the cell. Competition studies with APP indicated that its transport in L. plantarum and in Streptococcus faecalis was antagonized only by structurally related compounds such as glutamic, aspartic, and cysteic acids. Kinetic studies showed that APP was taken up by a single catalytic system in S. faecalis. A mutant strain of this organism which lacks one of two kinetically distinguishable dicarboxylic amino acid transport systems failed to accumulate measurable amounts of APP. These experiments indicate that the aminophosphonic acids are accumulated by the amino acid transport systems in these bacteria with minimal metabolic changes.

Amino Acids↗
PubMed1978

Purification and properties of pig brain guanine deaminase.

Guanine deaminase (guanine aminohydrolase, EC 3.5.4.3) from pig brain was purified to homogeneity by column chromatography and ammonium sulphate fractionation. Homogeneity was established by polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulphate (SDS). The molecular weight of 110 000 was determined by gel filtration and sucrose density gradient centrifugation. SDS polyacrylamide gel electrophoresis indicated subunits of a molecular weight of 50 000. The amino acid composition, the isoelectric point and the number of -SH groups were determined. 5.5'-Dithiobis-(2-nitrobenzoic acid) reacts with about seven -SH groups in the native enzyme, but upon denaturation with SDS, 10 -SH groups react with this former reagent. Using electrolytic reduction, 44 half-cystines were determined in accordance with the number of cysteic acid residues determined by amino acid analysis after performic acid oxidation. The Km values determined for substrates of the enzyme were 1.1 . 10(-5) M for guanine in 0.1 M Tris. HCl buffer (pH 8.0) and 3.3 . 10(-4) M for 8-azaguanine in 0.1 M phosphate buffer, pH 6.4. The pKa values determined for ionizable groups of the active site of the enzyme were near pH 6.2 and pH 8.2. The chemical and kinetic evidence suggests that cysteine and histidine may be essential for the catalysis.

Amino Acids↗
PubMed1978

Simplified two-step column-chromatographic determination of taurine in urine.

A two-step column-chromatographic procedure for accurate and rapid determination of taurine in urine is described. Sulfosalicyclic-acid deproteinized samples are chromatographed on a 0.9 X 10 cm column of cation-exchange resin (AG 50W-XB), with use of a pH 2.2 sodium citrate eluting buffer such that taurine and the more highly acidic compounds in urine are eluted in the void volume, and then on a 0.9 X 8 cm column of anion-exchange resin (AG 2-X8), from which taurine is preferentially eluted with 1 mol/liter acetic acid. The color developed with ninhydrin is directly proportional to taurine amounts as low as 0.01 mumol/sample. The method is highly reproducible, with analytical recoveries greater than 95%. The presence of 333 mumol of urea and 1 mumol of cysteic acid did not interfere in the analysis. When a mixture of C14-labeled amino acids other than taurine were co-chromatographed with taurine, less than 2% of the total counts loaded were located in the taurine fraction. Values for urinary taurine excretion by rats according to the present method agreed well with values obtained with an automated amino acid analyzer. Advantages of the present method for the determination of taurine are discussed.

Amino Acids↗
PubMed1991

Characterization of Rarobacter faecitabidus protease I, a yeast-lytic serine protease having mannose-binding activity.

Rarobacter faecitabidus protease I, a yeast-lytic serine protease, was characterized in order to elucidate the mechanism of lysis of yeast cells by this enzyme. The N-terminal amino acid sequence of the enzyme was found to be homologous to those of Lysobacter enzymogenes alpha-lytic protease and Streptomyces griseus proteases A and B around the catalytic His residue, showing that it is a mammalian type serine protease. In a study of its substrate specificity, it preferentially hydrolyzed the ester of alanine among amino acid p-nitrophenylesters. It also efficiently hydrolyzed succinyl Ala-Pro-Ala p-nitroanilide, the specific synthetic substrate for pancreatic elastase. With oxidized insulin B-chain, it hydrolyzed almost exclusively the peptide bond between valine 18 and cysteic acid 19 in the early step of the reaction, and thereafter it partially hydrolyzed Val12-Glu13, Ala14-Leu15, and Leu15-Tyr16. These results indicate that Rarobacter protease I is elastase-like in its substrate specificity, preferentially hydrolyzing the peptide bond of aliphatic amino acids. Its affinity for yeast cells was also investigated, and while Rarobacter protease I was adsorbed by yeast cells, pancreatic elastase was not. This difference was thought to account for the failure of pancreatic elastase to lyse yeast cells, even though its specificity is similar to that of the yeast-lytic enzyme. Rarobacter protease I was adsorbed by a mannose-agarose column and specifically eluted from the column with a buffer containing D-mannose or D-glucose. These monosaccharides also inhibited its yeast-lytic activity.(ABSTRACT TRUNCATED AT 250 WORDS)

Actinomycetales↗
PubMed1977

Isolation and amino acid sequence of COOH-terminal fragments from the beta subunit of human choriogonadotropin.

The amino acid sequence of the unique COOH-terminal region of the beta subunit of human choriogonadotropin has been reinvestigated. The desialylated subunit was digested with thermolysin and a 27-residue peptide from positions 115 through 141 isolated in a high yield. Quantitative Edman sequence degradation of this peptide, of another peptide produced by thermolysin digestion containing residues 142 to 145, and of two tryptic peptides (residues 123 to 145, 134 to 145) has established that the amino acid sequence of this region is: (formula: see text). In addition, the positions of attachment of the carbohydrate moieties to serine residues was established by a direct procedure using alkaline elimination and 35S-labeled sulfite addition, which yields [35S]-cysteic acid residues at the site of a substituted serine. Carbohydrate side chains in the COOH-terminal region have been shown to exist at residues 121, 127, 132, and 138. These studies have also resulted in the development of improved methods for the purification of COOH-terminal peptides of the human choriogonadotropin beta subunit.

Amino Acid Sequence↗
PubMed1975

Effects of several unusual sulfur-containing amino acids on rat liver cystathionine-gamma-lyase.

1. The mode of inhibition of rat liver cystathionine-gamma-lyase [L-cystathionine cysteine-lyase (deaminating), EC 4.4.1.1] was studied by using several unusual sulfur-containing amino acids newly found in this laboratory. Some cysteine conjugates (CMC, Beta-CEC, HCETC and HCPC) inhibited noncompetitively both homoserine dehydratase and diaminopropionate ammonia-lyase activities, and competitively gamma-cystathionase activity. CMTC exhibited a mixed type inhibition on both homoserine dehydratase and gamma-cystathionase activities, and a noncompetitive inhibition on the diaminopropionate ammonia-lyase activity. Some homocysteine conjugates (CMHC, beta-CEHC and HCEHC) inhibited competitively both the activity of homoserine dehydratase and of gamma-cystathionase, and exhibited a mixed type inhibition on the diaminopropionate ammonia-lyase activity. beta-CEC, CMHC and beta-CEHC were also effective inhibitors to cysteine desulfhydrase activity. 2. Among the other amino acids tested, DL-homocysteine and D-cysteine, irrespective of their concentration, exhibited a mixed type inhibition on the homoserine dehydratase activity. However, they promoted gamma-cystathionase activity at their lower concentrations and inhibited at their higher concentrations, more so than cystathionine. DL-alpha-Aminobutyric acid was a weak competitive inhibitor of the homoserine dehydratase, gamma-cystathionase and diaminopropionate ammonia-lyase activities. DL-alpha-Aminopimeric acid has the same chain length as beta-CEC, CMHC and CMTC, but it showed a very weak inhibitory effect compared with the latter sulfur-containing compounds. L-Methionine, DL-methionine sulfoxide, L-ethionine, L-cysteic acid, L-aspartic acid, L-asparagine, L-glutamic acid, L-glutamine, D-alanine, beta-alanine, L-ornithine and L-lysine had little or no effect on any activities of the enzyme preparation. These results were discussed in relation to the catalytic center of cystathionine-gamma-lyase.

Amino Acids, Sulfur↗
PubMed1975

The participation of methionine and cysteine in the formation of bonds resistant to the action of proteolytic enzymes in heated casein.

1. The influence of temperature, moisture content and the presence of glucose on the level of available methionine and cysteine in casein was studied. 2. Differences between total and available methionine and cysteine contents of heated casein (90 degrees for 24 h) were determined by an in vitro method. The maximum losses in total and available methionine content were 22 and 51% respectively. The losses in total and available cysteine content were 24 and 100% respectively. 3. The results indicated that for heated casein the release of amino acids by proteolytic enzymes was less complete than for native casein. 4. The results of rat growth assays suggested that diets containing oxidized casein are less well utilized by rats than those containing native casein. The decrease in body-weight of rats receiving the diets containing oxidized casein could be counteracted by the addition of methionine and 20 g unoxidized casein/kg diet. 5. There was a lower level of some available amino acids (determined after enzymic hydrolysis using pancreatopeptidase E (EC 3-4-4-7), leucine aminopeptidase (EC 3-4-I-I) and prolidase (EC 3-4-3-7)), including those essential for the rat, in oxidized casein as compared with native casein. 6. Cysteic acid, in oxidized casein, probably makes impossible the utilization of the amino acids in its neighbourhood. 7. From the differences in the available amino acid contents of the native, oxidized and heated casein it was concluded that the oxidation of casein causes the formation of complexes in the polypeptide chain, resistant to enzymic hydrolysis, but to a much lesser extent than does heating.

Amino Acids↗
PubMed1975

Protective action of ascorbic acid and sulfur compounds against acetaldehyde toxicity: implications in alcoholism and smoking.

Acetaldehyde is a toxic substance common to heavy drinking of alcohol and heavy smoking of cigarettes. It has been implicated thereby in diseases of the cardiovascular, respiratory, and central nervous systems. Protection against acetaldehyde toxicity (i.e. anesthesia and lethality) was studied in rats by oral intubation of test compounds 30-45 minutes prior to oral intubation of a standardized oral LD 90 dose (18 millimoles/kilogram) of acetaldehyde. Animals were monitored for anesthesia (loss of righting reflexes) and lethality for 72 hours. A total of 18 compounds was tested. L-ascorbic acid at 2 millimoles/kilogram (mM/kg) showed moderate protection against anesthesia and marked protection against lethality. Greatest protection against anesthesia and lethality was obtained at 2 m M/kg with each of the following: L-cysteine, N-acetyl-L-cysteine, thiamin-HCl, sodium metabisulfite, and L-cysteic acid. A combination of L-ascorbic acid with L-cysteine, and thiamin-HCl at reduced dose levels (2.0, 1.0 and 0.3 mM/kg, respectively) gave virtually complete protection. A detailed literature review is presented of the rationale and significance of these findings. Our findings could point the way to a possible build-up of natural protection against the chronic body insult of acetaldehyde arising from heavy drinking of alcohol and heavy smoking of cigarettes.

Acetaldehyde↗
PubMed1970

The composition of beta-lactamase I and beta-lactamase II from Bacillus cereus 569-H.

1. Crystalline beta-lactamase I from Bacillus cereus 569/H yielded only amino acids on acid hydrolysis, but crystalline beta-lactamase II from the same organism yielded also substantial quantities of neutral sugars and amino sugars. 2. Analysis with an amino acid analyser indicated that the two enzymes were similar though not identical in overall amino acid composition. Analysis of neutral and amino sugars as their silyl derivatives by gas-liquid chromatography showed that the carbohydrate moiety of beta-lactamase II contained residues of glucose, galactose, mannose, fucose, glucosamine and galactosamine. 3. After oxidation and hydrolysis both beta-lactamases gave small amounts of cysteic acid. After treatment of inactive Zn(2+)-free beta-lactamase II with N-ethylmaleimide or iodoacetate enzymic activity was not restored by the addition of Zn(2+).

Amino Acids↗
PubMed1993

Oxidative modification of inflammatory synovial fluid immunoglobulin G.

The release of highly reactive oxygen-derived products by activated phagocytic cells in inflammatory foci plays a major role in defense mechanisms against infection and in the generation of tissue injury. Oxidative modification of proteins in inflammatory foci may give rise to products that contribute to the perpetuation of inflammation. The present studies analyze the oxidative alterations of inflammatory synovial fluid immunoglobulin G (IgG). IgG was purified from the synovial fluids of five patients with rheumatoid arthritis and two patients with acute gouty arthritis by three sequential steps: gel filtration chromatography, immunoaffinity chromatography, and a final gel filtration chromatography step under dissociative conditions (4 M guanidine). The resulting protein peaks of > 150 kDa (pool I-1), 150 kDa (pools I-2 and II-2), and < 150 kDa (pools I-3 and II-3) were tested for the presence of a fluorescence profile distinctive of oxidized proteins, the peak corresponding to monomer IgG (pool II-2) was subjected to quantitative amino acid analysis, and the results were compared with a standard preparation of normal IgG oxidized with HOCl. In addition, the protein pools were tested for the presence of lipid peroxide products. The results indicate that a portion of the affinity-purified IgG formed high-molecular-mass covalently cross-linked aggregates as evidenced by its presence in the > 150-kDa pool after dissociatve gel filtration chromatography. Moreover, this fraction and the pool corresponding to monomer IgG (pool II-2) exhibited the fluorescence profile characteristic of oxidized proteins. Amino acid analysis of the monomer IgG fraction revealed decreases in the content of histidine, methionine, tyrosine, and cysteine, which were similar to the alterations measured in normal IgG oxidized by HOCl. The synovial fluid and standard oxidized IgG showed the presence of oxidative by-products of tyrosine (monochlorotyrosine) and cysteine (cysteic acid). The synovial fluid IgG yielded a novel component that was not present in the standard control or oxidized IgG. This component was partially identified by mass spectrometry. Finally, the smaller peptide fraction isolated from affinity-purified synovial fluid IgG (pools I-3 and II-3) only after the gel filtration chromatography step under dissociative conditions exhibited evidence of oxidative damage and the presence of high concentrations of thiobarbituric acid-reactive material (TBAR). These observations suggest that oxidative processes in inflammatory foci generate products derived from protein and lipids that may contribute to the self-perpetuation of inflammation.

Amino Acids↗
PubMed1991

Oxidation of spectrin and deformability defects in diabetic erythrocytes.

We reasoned that de novo oxidative damage, as a result of increased protein glycosylation, could participate in the mechanisms whereby diabetic erythrocytes acquire membrane abnormalities. To examine this hypothesis, the extent of erythrocyte membrane protein glycosylation and the oxidative status of spectrin, the major component of the erythrocyte membrane skeleton, were examined. Labeling erythrocyte membranes with [3H]borohydride, which labels glucose residues bound to proteins, revealed that several proteins were heavily glycosylated compared with nondiabetic erythrocyte membranes. In particular, the proteins beta-spectrin, ankyrin, and protein 4.2 were the most glycosylated. Although sodium dodecyl sulfate-polyacrylamide gel electrophoresis of diabetic erythrocyte membranes did not reveal any quantitative or qualitative abnormalities in spectrin or other membrane proteins, examination of spectrin oxidative status by amino acid analysis and with cis-dichlorodiammineplatinum(II) (cDDP), a chemical probe specific for protein methionine and cysteine residues, demonstrated that the diabetic spectrin was oxidatively damaged: spectrin from diabetic subjects contained 35% less methionine (P less than 0.002), 15% less histidine (P less than 0.006), and a twofold increase in cysteic acid (P less than 0.001) compared with normal spectrin. Diabetic spectrin bound 32% less cDDP than normal spectrin (P less than 0.001); the lowest cDDP binding was observed with spectrin from insulin-dependent diabetic subjects. The extent of cDDP binding to diabetic spectrin correlated moderately and inversely with glycosylated hemoglobin (GHb) levels (n = 12, r = -0.727). Erythrocyte deformability, measured by ektacytometry, was decreased between 5 and 23% of control measurements (average of approximately 10%) in 21 of 32 diabetic subjects surveyed.(ABSTRACT TRUNCATED AT 250 WORDS)

Aged↗