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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Polyglycine, polyalanine, polyleucine, poly-alpha-glutamic acid, poly-gamma-glutamic acid and poly-alpha-lysine were complexed with insulin under non denaturating conditions. The liberation behaviour of the hormone was investigated in vivo and in vitro in dependence of the insulin content, mole mass, ionic interaction and hydrophobicity of the polyamino acid. The in vitro results were mainly confirmed by animal experiments and indicated distinct effects of the physiochemical parameters to the bioavailability of insulin. The complex of poly-alpha-lysine and polyglycine were shown to be the most suited retard form, producing significant blood glucose lowering effects up to 12 hours.
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PMID:[Insulin polyamino acid complexes--a variable principle in the preparation of sustained-release forms]. 329 85

Inducible cadmium-binding proteins (Cd-BP) in the mussel, Mytilus edulis, were resolved into two molecular weight components, designated Cd-BP10 and Cd-BP20, by gel-permeation chromatography on Sephadex G-75. Each of these two molecular weight components were further resolved into four subcomponents by DEAE-ion-exchange chromatography. All eight subcomponents bound cadmium and exhibited significant UV absorption at 254 nm and little absorption at 280 nm. Each subcomponent was purified and subjected to amino acid composition analysis. Two classes were identified, one having higher cysteine (23.9-26.6 mole-%) and lower glutamic acid contents compared to the other class (11.6-18.2 mole-% cysteine). All subcomponents have a relatively high glycine content (approximately 15 mole-%) relative to mammalian metallothioneins (approximately 8 mole-%). Although the Cd-BP20 have apparent molecular weights almost twice the Cd-BP10, the exact molecular relationship between these binding proteins is not known.
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PMID:Cadmium-binding proteins in the mussel, Mytilus edulis. 370 63

The availability of epsilon-lysine residues of apolipoprotein B in LDL for chemical or enzymic modification was investigated. Amino acid analyses of detergent-solubilized apolipoprotein B, following cyanoethylation with acrylonitrile, revealed that 10% of the lysine in apolipoprotein B were unreactive. The unreactive residues were associated with the most hydrophobic subfraction of apolipoprotein B. Since apolipoprotein B has a high molecular weight a study was undertaken to determine whether lysine residues were crosslinked to glutamic acid via epsilon-(gamma-glutamyl)lysine as demonstrated for fibrin. Apolipoprotein B was digested exhaustively with proteases. The content of epsilon-(gamma-glutamyl) lysine was determined by chromatography and isotope dilution. In contrast to earlier reports for serum LDL the data showed that less than 0.01 moles of lysine/mole of LDL apolipoprotein B were present as epsilon-(gamma-glutamyl)lysine in plasma LDL. It was determined also that the crosslinks were not found in apolipoprotein B during clotting since LDL was not a substrate for clotting factor XIII which forms the bond in fibrin. Furthermore, the lipoprotein contained no inherent transglutaminase activity. It is concluded that the lysine residues in LDL, which are unreactive to cyanoethylation, can not be detected in the digests as epsilon-(gamma-glutamyl)lysine.
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PMID:The biochemistry of epsilon-amino groups of lysine residues from apolipoprotein B of human low density lipoprotein. 373 52

1. The cyst wall of Colpoda steinii has been isolated and its chemical nature examined. It had a nitrogen content 13.9+/-0.2% (s.d.) and an ash 8.6+/-1.6% (s.d.). After lipid and hot-acid extraction there was a variable residual phosphorus of 0.19-0.64%. The protein nature, indicated by infrared and ultraviolet absorption, was confirmed when 100mug. of hydrolysed wall gave a ninhydrin colour equivalent to that given by 0.88-1.01mumoles of glycine. Hexosamine, hexose, pentose, lipid and dipicolinic acid were absent. 2. Paper chromatography of hydrolysates, besides showing the presence of the usual protein amino acids and three unidentified ninhydrin-reacting spots, indicated the presence of large amounts of glutamic acid. Estimated by chromatography, the amount present was 52.9+/-0.6 (s.d.) g./100g. of ash-free wall; manometric estimation of l-glutamic acid with l-glutamate 1-carboxy-lyase gave 46.5+/-0.9 (s.d.) g./100g. 3. Free carboxyl groups were estimated by titration as 0.159+/-0.011 (s.d.) mole/100g. and those present as amide as 0.154+/-0.004 (s.d.) mole/100g., and the total was compared with the dicarboxylic acid content 0.360+/-0.010 (s.d.) mole/100g. 4. After treatment with 98% formic acid 25-30% of the wall material could be extracted by 0.05m-sodium carbonate solution (extract 1); after treatment of the residue with performic acid a further 62-63% based on the original weight could be extracted by 0.05m-sodium carbonate (extract 2). 5. The average values found for the glutamic acid contents were 21.7g./100g. for extract 1 and 58.0g./100g. for extract 2. The cysteic acid content of whole oxidized wall was about 5.8g./100g. and of extract 2 also about 5.8g./100g. The glutamic acid and cysteic acid contents of the final residue were also investigated. 6. The significance of these extraction experiments in relation to the wall structure is discussed.
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PMID:The cyst wall of Colpoda steinii. A substance rich in glutamic acid residues. 495 13

1. The mucopeptide component of wall preparations from Bacillus licheniformis was obtained in soluble form by treatment of the acid-insoluble residue of walls with lysozyme. 2. The soluble mucopeptide contains glutamic acid, diaminopimelic acid, alanine, N-acetylglucosamine and N-acetylmuramic acid in the molecular proportions 1.0:1.0:1.6:0.8:0.7. In addition approx. 1 mole of amide/mole of glutamic acid is present. Essentially all of the dry weight and nitrogen content of soluble mucopeptide is accounted for by these constituents. 3. The optical configurations of the amino acids were determined. Approx. 0.6 mole of d-alanine and 1.0 mole of l-alanine are present/mole of glutamic acid. 4. The structures of several small peptides derived from soluble mucopeptide after mild acid hydrolysis were established. 5. The structure of soluble mucopeptide from B. licheniformis is discussed on the basis of these results together with data on the number of free amino groups present in soluble mucopeptide.
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PMID:The cell wall of Bacillus licheniformis N.C.T.C. 6346. Composition of the mucopeptide component. 572 70

Autolysis of isolated cell walls of Staphylococcus aureus strain Copenhagen was accompanied by the release of 1 mole of N-terminal alanine per mole of glutamic acid. No other N-terminal amino acids and no C-terminal amino acids were released. These observations indicated that complete hydrolysis of N-acetylmuramyl-l-alanine linkages ("amidase" action) had occurred. This was confirmed by fractionation and analysis of the products. Hydrolysis of 4-O-beta-N-acetylglucosaminyl-N-acetylmuramic acid linkages also occurred to a variable extent; on one occasion, complete degradation to disaccharides and hexosamine-free polypeptides (with intact pentaglycine cross-bridges) occurred. In one other instance, hydrolysis within pentaglycine bridges also occurred. Analyses of intact cell walls indicated that, in vivo, glycine endopeptidase activity was negligible and amidase activity was low, but that endo-beta-N-acetylglucosaminidase hydrolysed about 8% of the N-acetylglucosaminyl-N-acetylmuramic acid linkages. Autolysis of isolated cell walls was too slow for the enzymes isolated with them to have significant action during this isolation. The possible functions of these autolytic activities are discussed.
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PMID:Mechanism of autolysis of isolated cell walls of Staphylococcus aureus. 577 31

Mucopeptides isolated from Streptococcus bovis cell walls were found to be composed of alanine, glutamic acid, lysine, and threonine in a mole ratio of 3:1:1:1. A dipeptide, N(epsilon)-lysylthreonine, was isolated from S. bovis mucopeptide by ion-exchange chromatography. This finding suggests that threonine is associated with the bridge which cross-links adjacent tetrapeptides by connecting the epsilon-amino group of lysine of one tetrapeptide to the carboxyl group of d-alanine of another to form the mucopeptide matrix.
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PMID:Chemical studies on the structure of mucopeptide isolated from Streptococcus bovis. 580 3

The response of mice to synthetic linear polypeptides of known composition but random sequence has been studied. Neither Swiss mice nor a number of inbred strains could respond to copolymers of only 2 amino acids (G(60)L(40), G(60)A(40), G(90)T(10)). Upon introduction of as little as 4 mole per cent of a third amino acid, good immune responses were obtained, regardless of the nature of the third amino acid. The level of the immune response to a series of glu-lys-ala polymers increased with increasing alanine content of the polymer.
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PMID:Antigenicity of polypeptides (poly alpha amino acids). XV. Studies on the immunogenicity of synthetic polypeptides in mice. 584 32

The ability of mice to form antibodies against the random terpolymer glu(57)lys(38)ala(5) is controlled by a codominant Mendelian factor. Three of 7 inbred strains were 100 per cent responders; the others were completely negative. All of these strains could make antibody to related polymers with higher alanine content (10 and 40 mole per cent). Breeding studies using the progeny of Swiss mice indicated that a similar genetic factor was involved.
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PMID:Antigenicity of polypeptides (poly alpha amino acids). XVI. Genetic control of immunogenicity of synthetic polypeptides in mice. 584 33

Streptococcal mucopeptide, solubilized by either ultrasonic treatment or lysozyme, gave a precipitin reaction with rabbit antimucopeptide serum. A haptenic inhibitor of this reaction, which was composed of alanine, glutamic acid, and lysine in a mole ratio of 4:1:1, was isolated from a Streptomyces albus enzymes digest of Group D cell walls by ion exchange chromatography. When selected antisera were employed, greater than 90% inhibition of the mucopeptide quantitative precipitin reaction was achieved with 2 mg/ml of this inhibitor, whereas a hexosamine fraction with minimal concentrations of amino acid residues was inactive in this respect. These results suggest that the peptide moiety is an antigenic determinant of mucopeptide. Preliminary results indicate that the hexosamine polymer of the mucopeptide is a secondary antigenic determinant.
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PMID:Studies on the immunochemistry of streptococcal mucopeptide. 591 89


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