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Query: UMLS:C0847097 (acidity)
 15,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Proton magnetic resonance studies of the acid-base chemistry of the glycyl ammonium, histidyl imidazolium, and lysyl ammonium groups of glycyl-L-histidyl-L-lysine and of the glycyl ammonium and histidyl imidazolium groups of glycyl-L-histidine and glycyl-L-histidylglycine are described. Chemical-shift data indicate that, at the molecular level, the glycyl ammonium and the histidyl imidazolium groups are titrated over the same pH range, with the acidity of the imidazolium group some 8 to 10 times that of the glycyl ammonium group, depending on the peptide. The lysyl ammonium group of Gly-His-Lys is much less acidic and is titrated over a higher pH range. Microscopic and macroscopic acid-dissociation constants were determined from chemical-shift data for each of the peptides. It is shown how microscopic formation constants for protonated metal complexes of these ligands, which are being used increasingly as models for the binding of metal ions by proteins, can be calculated from the macroscopic formation constants and the microscopic acid-dissociation constants. The acid-base chemistry of Gly-His-Lys is discussed with respect to its recently discovered biological activity.
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PMID:Determination of the microscopic and macroscopic acid dissociation constants of glycyl-L-histidyl-L-lysine and related histidine peptides. 1 68

Studies have been made on the amino acid composition of electrophoretically homogeneous albumin and its main isoelectrically homogeneous fraction in two strains of hens and their hybrid. Serum albumin of hen and hybrid is characterized by higher total content of Asp and Glu residues as compared with that of the cock (137, 121, and 116 respectively) and lower content of Lys (59 against 66). The acidity of albumin increases in the line cock-hen-hybrid. With respect to its amino acid composition, the maternal serum albumin stands close to the hybrid one.
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PMID:[Amino acid composition of chicken serum albumin]. 66 8

Studies have been made on the amino acid composition of electrophoretically homogeneous albumin and its main isoelectrically homogeneous fraction in two strains of hens and their hybrid. Serum albumin of hen and hybrid is characterized by higher total content of Asp and Glu residues as compared with that of the cock (137, 121, and 116 respectively) and lower content of Lys (59 against 66). The acidity of albumin increases in the line cock-hen-hybrid. With respect to its amino acid composition, the maternal serum albumin stands close to the hybrid one.
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PMID:[Hemoglobin oxygen affinity in Mesocricetus auratus hamsters of different ages]. 66 10

The effects of opaque-2 corn and the complementation with lupin flour on the sensory quality and nutritive value of "humitas" were evaluated. Moreover, the nutritional and quality changes which occur during the retorting of the product canned in two can sizes, were studied. Hybrid and opaque-2 corn were replaced with 6%, 8%, 10% and 12% lupin flour, being 8% the complementation level with the best sensory and nutritional quality. Heat penetration studies of the product canned in N2 and N6 tin cans, were carried out. Total process time at 121 degrees C was 73 min and 147 min, respectively. "Humitas" prepared with hybrid and opaque-2 corn, with and without 8% lupin flour, prior and after sterilization, were subjected to proximate analysis, pH, titratible acidity and available lysine determinations. Biological evaluation of the protein by the net protein ratio (NPR) and digestibility, as well as organoleptic quality and acceptability analyses were also determined. It was concluded that the complementation with 8% lupin flour improves significantly the nutritional value of hybrid corn "humitas", but not that of opaque-2 corn. The canning process affected lysine availability and was directly related to the amino acid concentration, and to the retorting duration. On the other hand, the thermal processing adversely affected the biological quality of protein and some sensory attributes. The 8% lupin complementation was also detrimental for the organoleptic quality of the product.
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PMID:[Canning of "humitas" prepared with opaque-2 corn, supplemented with sweet lupine (Lupinus albus var. Multolupa). Nutritional and quality changes]. 248 29

The potential contribution of thiolimidate formation to the increased kinetic acidity of the alpha-proton of acetyl-CoA in the carbon-carbon bond forming reaction catalyzed by 3-ketoacyl-CoA thiolase (thiolase I) from porcine heart was assessed by chemical modification and isotope exchange experiments. Thiolase is only partially inactivated after the chemical modification of lysine residues by reductive methylation, pyridoxal phosphate, or o-phthaldehyde (specific for vicinal lysine and cysteine). The thiolase-catalyzed formation of acetyl-CoA from acetoacetyl-CoA and CoASH in 18OH2 is not accompanied by the appearance of 18O in the acetyl-CoA product. These experiments effectively rule out participation of thiolimidate formation in the thiolase reaction. Other mechanisms must be employed to facilitate the abstraction of the alpha-proton of acetyl-CoA by thiolase I.
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PMID:Examination of the role of thiolimidate formation in the cleavage of acetoacetyl-CoA catalyzed by thiolase I from porcine heart. 256 19

Affinity labeling and comparative sequence analyses have placed Lys-166 of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at the active site. The unusual nucleophilicity and acidity of the epsilon-amino group of Lys 166 (pKa = 7.9) suggest its involvement in catalysis, perhaps as the base that enolizes ribulosebisphosphate (Hartman, F.C., Milanez, S., and Lee, E.H. (1985) J. Biol. Chem. 260, 13968-13975). In attempts to clarify the role of Lys-166 of the carboxylase, we have used site-directed mutagenesis to replace this lysyl residue with glycine, alanine, serine, glutamine, arginine, cysteine, or histidine. All seven of these mutant proteins, purified by immunoaffinity chromatography, are severely deficient in carboxylase activity; the serine mutant, which is the most active, has a kcat only 0.2% that of the wild-type enzyme. Although low, the carboxylase activity displayed by some of the mutant proteins proves that Lys-166 is not required for substrate binding and argues that the detrimental effects brought about by amino acid substitutions at position 166 do not reflect gross conformational changes. As demonstrated by their ability to tightly bind a transition-state analogue (2-carboxyarabinitol 1,5-bisphosphate) in the presence of CO2 and Mg2+, some of the mutant proteins undergo the carbamylation reaction that is required for activation of the wild-type enzyme. Since Lys-166 is required neither for activation (i.e. carbamylation by CO2) nor for substrate binding, it must be essential to catalysis. When viewed within the context of previous related studies, the results of site-directed mutagenesis are entirely consistent with Lys-166 functioning as the base that initiates catalysis by abstracting the C-3 proton from ribulosebisphosphate. An alternative possibility that Lys-166 acts to stabilize a transition state in the reaction pathway cannot be rigorously excluded.
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PMID:Function of Lys-166 of Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase as examined by site-directed mutagenesis. 310 87

Conditions were determined in which approximately one mole of omicron-phthalaldehyde reacts with one mole of aldolase subunit yielding a stable fluorescent isoindole derivative. During this chemical modification, a linear relationship was observed between the enzyme inactivation and absorbance change (337 nm) or fluorescence change (lambda em 420 nm, and lambda ex 338 nm) characteristic for isoindole ring formation. The reaction follows second-order kinetics, k = 1.1 X 10(3) M-1 S-1, in 50 mM borate buffer, pH 8.4 at 25 degrees C. The modification of aldolase results in loss of approximately one -SH group per protein subunit. The enzyme is protected against modification by substrates and competitive inhibitors. Essentially no isoindole derivative is formed when the glycerol-1-phosphate-lysyl derivative of aldolase is used for modification studies. It is concluded that aldolase modification occurs at the active-site region. Isolation of cross-linked peptides suggests that Lys-227 and Cys-336 are involved in formation of the isoindole derivative. This result supports Cys-336 as the active-site cysteine necessary for aldolase catalytic activity. Fluorescence studies have shown that the isoindole group linked to aldolase has its lambda max, em markedly shifted toward shorter wavelength in comparison to the fluorescence of free isoindole derivatives in aqueous solution. In model studies a linear relationship between lambda max, em of 1-(beta-hydroxyethylthio)-2-beta-hydroxyethylisoindole and the solvent polarity or acidity was observed. The results of the studies suggest that the microenvironment of the cleft in aldolase which binds isoindole appears to be of low acidity and low polarity. The apparent low polarity experienced by the isoindole probe may be due to its location in an actual low-polarity portion of the active site, or may be due to non-relaxing surroundings of the probe.
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PMID:o-Phthalaldehyde, a fluorescence probe of aldolase active site. 666 5

The resorbable polymers polyglycolic acid (PGA) and polylactic acid (PLA) are gaining increasing importance in tissue engineering and cell transplantation. The present investigation was focused on the biocompatibility and cell retaining behavior of PGA/poly-L-lactide (PLLA) (90/10) and PLLA nonwoven structures for the in vitro development of chondrocyte-polymer constructs. The effect of the relevant monomers to chondrocytes was analyzed. Type II collagen and poly-L-lysine were compared to improve loading of PGA/PLLA and PLLA polymer nonwovens with chondrocytes. The 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetra-zoliumbrom ide (MTT) test was applied for quantification. At concentrations above 2 mg/mL, glycolic acid was more cytotoxic than lactic acid. As shown by pH equilibration, the cytotoxic effect is not due merely to the acidity of the alpha-hydroxy acids. Regarding the degradation products, glycolic acid, and L(+) lactic acid, nonwovens of PLLA are more biocompatible with chondrocytes than nonwovens of polyglycolide. Collagen type II and poly-L-lysine generally improved cell seeding on resorbable polymers in tissue engineering; however, their efficiency varies depending on the type of fiber structure.
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PMID:Resorbable polyesters in cartilage engineering: affinity and biocompatibility of polymer fiber structures to chondrocytes. 873 23

2D-NMR experiments were used to determine the pKa values ranging from 8.0 to >/=11.1 of seven basic residues in turkey ovomucoid third domain (OMTKY3) and were compared to values predicted as described by Antosiewicz et al. [(1996) Biochemistry 35, 7819-7833]. Lys 13, 29, and 34 were previously attributed with increasing the acidity of numerous acidic residues [Schaller, W., and Robertson, A. D. (1995) Biochemistry 34, 4714-4723]. These interactions were expected to raise the pKa values of those basic groups; however, the pKa values of Lys 13 and 34 are less than the model compound values. The pKa values of the other basic residues are greater than the model compound values and, unlike the acidic residues, all are surprisingly insensitive to salt. While the calculations properly predict the direction of most of the pKa shifts and provide valuable insight into the possible molecular origins of the interactions that perturb pKa values, there is a tendency to overestimate the magnitude of the shifts and their salt dependence. Interestingly, the shapes of both the calculated and observed transitions are often more complex than expected for a simple titration, suggesting that pKa values at many sites are changing during the transition. Differences between predicted and experimental pKa values and titration profiles for some residues may be due to as yet uncharacterized structural changes at the extremes of pH.
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PMID:Theoretical and experimental analysis of ionization equilibria in ovomucoid third domain. 962 26

Growth of, and acid production by Bifidobacterium lactis and Lactobacillus acidophilus using ovine and caprine milk as media were evaluated for their potential use in cheese-making. A protein hydrolysate (MHP, obtained from incubation of bovine milk with protease) or a mixture of free amino acids (FAA, similar to the amino acid fraction of MHP) was added as a nitrogen enrichment source. Bifidobacterium lactis and Lact. acidophilus were inoculated at 50 ml l-1 and incubated at 37 degrees C with growth supplements added at ratios in the range 25-50 ml l-1. The maximum viable counts of Bif. lactis were lower in plain ovine and caprine milk than in nitrogen-enriched milk, and MHP was a better growth promoter than FAA. A similar trend was observed with the acidity values developed, and attempts to correlate growth with acidity were successfully performed. The highest uptake rates of amino acids in ovine milk were observed for lysine, isoleucine, leucine and proline, but only isoleucine was taken up at a similar rate in caprine milk. Final bacterial viable counts of Lact. acidophilus in the plain and enriched forms of ovine milk did not differ greatly from each other, although FAA was statistically a better growth promoter than MHP. Unlike results in ovine milk, cultures of Lact. acidophilus in caprine milk exhibited drops of 1-1.5 log cycles in viable cell counts by 24 h of fermentation, irrespective of the nature of the nitrogen source. Parallel studies indicated that the excess of fatty acid residues in caprine milk could be responsible for the poor growth of Lact. acidophilus.
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PMID:Use of small ruminants' milk supplemented with available nitrogen as growth media for Bifidobacterium lactis and Lactobacillus acidophilus. 983 Jan 19


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