scholarly journals The products of the partial acid hydrolysis of the mucopeptide from cell walls of Micrococcus lysodeikticus

1959 ◽  
Vol 72 (4) ◽  
pp. 647-654 ◽  
Author(s):  
H R Perkins ◽  
H. J. Rogers
Keyword(s):  
Acid Hydrolysis ◽  
Cell Walls ◽  
Partial Acid Hydrolysis ◽  
Micrococcus Lysodeikticus ◽  
Hydrolysis Of

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.

Phosphopeptides Obtained by Partial Acid Hydrolysis of α-Casein2

1957 ◽  
Vol 79 (10) ◽  
pp. 2559-2565 ◽  
Author(s):  
N. J. Hipp ◽  
M. L. Groves ◽  
T. L. McMeekin
Keyword(s):  
Acid Hydrolysis ◽  
Partial Acid Hydrolysis ◽  
Hydrolysis Of

scholarly journals A study of the acidic peptides formed on the partial acid hydrolysis of wool

1949 ◽  
Vol 44 (5) ◽  
pp. 548-560 ◽  
Author(s):  
R. Consden ◽  
A. H. Gordon ◽  
A. J. P. Martin
Keyword(s):  
Acid Hydrolysis ◽  
Partial Acid Hydrolysis ◽  
Acidic Peptides ◽  
Hydrolysis Of
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