scholarly journals Bacteriolytic enzymes from Staphylococcus aureus. Specificity of action of endo-β-N-acetylglucosaminidase

1970 ◽  
Vol 120 (4) ◽  
pp. 735-744 ◽  
Author(s):  
T. Wadström ◽  
K. Hisatsune
Keyword(s):  
Amino Acids ◽  
Staphylococcus Aureus ◽  
Acid Hydrolysis ◽  
Cell Walls ◽  
Muramic Acid ◽  
Bacteriolytic Enzymes ◽  
Bacteriolytic Enzyme ◽  
Enzyme Digest ◽  
Micrococcus Lysodeikticus ◽  
Hydrolysis Of

The bacteriolytic enzyme with an isoelectric point of 9.5 that is produced by all strains of Staphylococcus aureus investigated was purified from strain M18 (Wadström & Hisatsune, 1970). This enzyme released reducing groups from cell walls of Micrococcus lysodeikticus and was thus shown to be a bacteriolytic hexosaminidase. Although dinitrophenylation and acid hydrolysis of cell walls hydrolysed by a partially purified enzyme gave DNP-alanine and DNP-glycine from staphylococcal peptidoglycan, which indicated the presence of a peptidase and probably also an N-acetylmuramyl-l-alanine amidase, hydrolysis of cell walls by the extensively purified enzyme did not give any DNP-amino acids. The enzyme digest was purified by Amberlite CG-120 and Sephadex G-10 chromatography. Reduction by sodium borohydride of the disaccharide obtained was followed by acid hydrolysis and paper chromatography. Glucosamine completely disappeared after this treatment and a new spot identical with glucosaminitol appeared. The muramic acid spot remained unchanged. The purified enzyme was found to be devoid of exo-β-N-acetylglucosaminidase activity. These results are compatible with the action of a bacteriolytic endo-β-N-acetylglucosaminidase. It is also proposed that this enzyme is probably identical with the staphylococcal lysozyme. The mode of action of this has not previously been investigated.

Structure and composition of the alkali-insoluble cell wall fraction of Coprinus macrorhizus var. microsporus

1980 ◽  
Vol 58 (2) ◽  
pp. 147-153 ◽  
Author(s):  
Carey B. Bottom ◽  
Donald J. Siehr
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Acid Hydrolysis ◽  
Cell Walls ◽  
Cell Wall Fraction ◽  
Enzymic Hydrolysis ◽  
Methylation Analysis ◽  
Partial Acid Hydrolysis ◽  
The Core ◽  
Hydrolysis Of

The alkali-insoluble (R-) fraction from the cell walls of Coprinus macrorhizus var. microsporus is a highly branched glucan, containing α-(1 → 4), β-(1 → 3), and β-(1 → 6) linkages as shown by methylation, partial acid hydrolysis, and enzymic hydrolysis. The α-(1 → 4)-linked segments are joined by occasional β-(1 → 3) links as suggested by the identification of 2-O-α-glucopyranosyl erythritol in the hydrolysate of the reduced, periodate-oxidized glucan. Hydrolysis of the permethylated glucan gave nearly equimolar amounts of 2,4-di- and 2,3-di-O-methyl-D-glucose. Methylation analysis of the residue from enzymic hydrolysis, the "CORE-fraction," indicated the presence of glucose residues in this fraction linked through positions O1, O3, O4, and O6. Hydrolysates of the R-fraction contained mannose, glucosamine, and amino acids in addition to glucose.

scholarly journals Acid Hydrolysis of Phenylthiohydantoins of Amino Acids

1971 ◽  
Vol 24 (4) ◽  
pp. 1247 ◽  
Author(s):  
AS Inglis ◽  
PW Nicholls ◽  
CM Roxburgh
Keyword(s):  
Amino Acids ◽  
Hydrochloric Acid ◽  
Thin Layer ◽  
Acid Hydrolysis ◽  
Free Amino ◽  
Hydriodic Acid ◽  
Ultraviolet Spectroscopy ◽  
Quantitative Identification ◽  
Layer Chromatography ◽  
Hydrolysis Of

The phenylthiohydantoins (PTHs) derived from amino acids were hydrolysed in boiling hydriodic acid for 24 hr. Good yields of free amino acids were obtained for all PTH derivatives except methionine. In contrast to hydrolysis with hydrochloric acid, hydrolysis with hydriodic acid converts PTH-threonine, PTH-serine, and PTH-tryptophan respectively to oc-amino-n-butyric acid, alanine, and a mixture (approx. 2: 1) of glycine and alanine. This procedure provides a useful adjunct to thin-layer chromatography and ultraviolet spectroscopy for quantitative identification of the PTH derivative.

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

Improved continuous-flow method for detemination of total serum hexosamines.

1976 ◽  
Vol 22 (8) ◽  
pp. 1394-1396 ◽  
Author(s):  
P Z Sobocinski ◽  
W J Canterbury ◽  
K H Jurgens
Keyword(s):  
Amino Acids ◽  
Acid Hydrolysis ◽  
Continuous Flow ◽  
Total Serum ◽  
Manual Method ◽  
Flow Method ◽  
Hydrolysis Of ◽  
Automated Determination ◽  
Continuous Flow Method

Abstract We describe an automated determination of serum hexosamine by the Elson-Morgan reaction, together with reagent modifications that minimiz interference from amino acids and sugars present in acid hydrolysates of sera. We used a novel 15-min autoclave procedure for the acid hydrolysis of sera before analysis to facilitate the detemination as compared to the 4-h hydrolysis used in the conventional manual method. Results correlated well (r = 0.906) with those obtained by the corresponding manual method.

THE SYNTHESIS OF D,L-α-AMINO-ε-HYDROXYCAPROIC ACID AND A NEW SYNTHESIS OF D,L-LYSINE

1948 ◽  
Vol 26b (4) ◽  
pp. 387-392 ◽  
Author(s):  
Roger Gaudry
Keyword(s):  
Amino Acids ◽  
Acid Hydrolysis ◽  
Hydrobromic Acid ◽  
Starting Material ◽  
New Synthesis ◽  
Strecker Synthesis ◽  
Hydrolysis Of ◽  
Bromo Compound

δ-Hydroxyvaleraldehyde, obtained by acid hydrolysis of dihydropyran, is a convenient starting material for the synthesis of D,L-lysine. Application to the aldehyde of the Bucherer modification of the Strecker synthesis for α-amino acids yields 5-δ-hydroxybutylhydantoin which is hydrolyzed into D,L-α-amino-ε-hydroxycaproic acid. D,L-Lysine is obtained from 5-δ-hydroxybutylhydantoin by bromination with hydrobromic acid into 5-δ-bromobutylhydantoin, amination of the bromo compound with ammonia, and hydrolysis of the hydantoin ring into D,L-lysine, readily isolated as the dipicrate.

scholarly journals STUDIES ON THE CHEMISTRY AND IMMUNOCHEMISTRY OF CELL WALLS OF STAPHYLOCOCCUS AUREUS

1962 ◽  
Vol 116 (2) ◽  
pp. 229-245 ◽  
Author(s):  
Stephen I. Morse
Keyword(s):  
Staphylococcus Aureus ◽  
Glutamic Acid ◽  
Cell Walls ◽  
Antigenic Determinant ◽  
Intact Cell ◽  
Teichoic Acid ◽  
The Other ◽  
Aureus Strain ◽  
Muramic Acid ◽  
Sheep Erythrocytes

The cell walls of an 80/81 strain of Staphylococcus aureus (NYH-6) contain alanine, glycine, glutamic acid, lysine, muramic acid, glucosamine, and ribitol phosphate. 94 per cent of the phosphorus and 41 per cent of the glucosamine are removed by extraction of the cell walls with hot 5 per cent TCA, but significant amounts of the other constituents are not extracted by this procedure. The residue after hot TCA extraction (mucopeptide) is susceptible to lysozyme whereas the intact cell walls are resistant. Staphylococcus aureus cell walls are agglutinated by S. aureus antisera. Agglutination of the cell walls of one S. aureus strain is inhibited by absorption of antisera with cell walls of other S. aureus strains but not by absorption with S. albus cell walls. The ribitol teichoic acid can be isolated from cold TCA extracts of the cell walls. This compound consists almost entirely of ribitol phosphate and glucosamine. The isolated teichoic acid of strain NYH-6 is readily fixed to tanned sheep erythrocytes and these sensitized cells are agglutinated by S. aureus antisera. Cold TCA extracts of cell walls of other strains of S. aureus inhibit hemagglutination whereas extracts of S. albus walls do not. Studies on the inhibition of both hemagglutination and precipitation indicate that the antigenic determinant of S. aureus NYH-6 teichoic acid is ß-N-acetylglucosamine.

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