The Resolution of Amino Acids by Enzymes Part 1: Proteolytic Enzyme Bromelain for Hydrolysis ofL-Amino Acid Methyl Esters

1977 ◽  
Vol 24 (3) ◽  
pp. 129-133 ◽  
Author(s):  
Chi-Huey Wong ◽  
Shui-Tien Chen ◽  
Kung-Tsung Wang
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Proteolytic Enzyme ◽  
Methyl Esters ◽  
Acid Methyl ◽  
Amino Acid Methyl Esters

Multifunctional lubricant additives derived from natural amino acids and methyl oleate

RSC Advances ◽  
2015 ◽  
Vol 5 (95) ◽  
pp. 77538-77544 ◽  
Author(s):  
Arukali Sammaiah ◽  
Korlipara V. Padmaja ◽  
Shiva Shanker Kaki ◽  
Rachapudi B. N. Prasad
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Methyl Oleate ◽  
Thioglycolic Acid ◽  
Methyl Esters ◽  
Lubricant Additives ◽  
Acid Methyl ◽  
Multifunctional Additives ◽  
Natural Amino Acids ◽  
Amino Acid Methyl Esters

Novel multifunctional additives were synthesized from methyl oleate via thioglycolic acid addition followed by condensation with different amino acid methyl esters.

Chiral recognition of amino-acid esters by a glucose-derived macrocyclic receptor

2021 ◽  
Author(s):  
Pit Dominique ◽  
Martin Schnurr ◽  
Bartosz Lewandowski
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Chiral Recognition ◽  
Methyl Esters ◽  
Aqueous Environment ◽  
Amino Acid Esters ◽  
Acid Methyl ◽  
Wide Range ◽  
Acid Esters ◽  
Amino Acid Methyl Esters

We report a glucose-based crown ether capable of chiral recognition of a wide range of amino-acid methyl esters in aqueous environment. The enantioselectivities towards amino-acids with extended hydrophobic side chains...

scholarly journals Responses of cultured cardiac myocytes to lysosomotropic compounds and methylated amino acids

1985 ◽  
Vol 74 (1) ◽  
pp. 119-135
Author(s):  
R.S. Decker ◽  
M.L. Decker ◽  
V. Thomas ◽  
J.W. Fuseler
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Methyl Ester ◽  
Acridine Orange ◽  
Cardiac Myocytes ◽  
Methyl Esters ◽  
Acid Proteinase ◽  
Weak Bases ◽  
Acid Methyl ◽  
Amino Acid Methyl Esters

Cardiac myocytes whose lysosomes had been pre-labelled with acridine orange were exposed to either L-amino acid methyl esters (L-leucine or methionine methyl ester) or to ‘lysosomotropic’ weak bases (chloroquine, methylamine, and NH4Cl) for 1 h. Both types of interventions dilated lysosomes equally and inhibited proteolysis to varying degrees. The weak bases produced no apparent alterations in the acridine orange staining, whereas the methylated amino acids induced a marked redistribution of the fluorescent dye from lysosomes into the myoplasm, suggesting that they may have provoked a change in lysosomal membrane permeability. A brief exposure to weak bases failed to enhance acid proteinase secretion into the culture medium but apparently inactivated cellular cathepsin B activity. In contrast, methylated amino acids induced no alterations in acid proteinase activity or the cellular distribution of the two proteolytic enzymes. Lastly, weak bases markedly elevated intralysosomal pH as measured with fluorescein dextran, while only modest rises were observed after amino acid methyl ester treatment. The present observations imply that amino acid methyl esters represent a new class of reagents with actions distinctly different from those of chloroquine and NH4Cl, and they may provide a unique and valuable means of studying secondary lysosomal function in cell culture.

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