sodium-dodecyl-sulfate and n-hexanal

sodium-dodecyl-sulfate has been researched along with n-hexanal* in 1 studies

Other Studies

1 other study(ies) available for sodium-dodecyl-sulfate and n-hexanal

Article	Year
Kinetics of amino acid esterification catalyzed by hydrophobic derivatives of alpha-chymotrypsin. Biochimica et biophysica acta, 1987, Jan-30, Volume: 911, Issue:2 Hexyl-alpha-chymotrypsin, a hydrophobic derivative of the enzyme, is explored for the proteinase-catalyzed ester synthesis reaction with N-acetyl-L-tyrosine and ethanol. To guarantee the preservation of the enzyme activity and to allow for the extraction of the product in the organic phase, a biphasic system was used. The Vm increased for the modified enzyme. This phenomenon was linked to the modification of the protein as demonstrated by its chemical denaturation with sodium dodecyl sulfate. Topics: Aldehydes; Amino Acids; Chemical Phenomena; Chemistry; Chymotrypsin; Kinetics; Protein Denaturation; Sodium Dodecyl Sulfate; Structure-Activity Relationship; Tyrosine	1987

Article

Year

Kinetics of amino acid esterification catalyzed by hydrophobic derivatives of alpha-chymotrypsin.

Biochimica et biophysica acta, 1987, Jan-30, Volume: 911, Issue:2

Hexyl-alpha-chymotrypsin, a hydrophobic derivative of the enzyme, is explored for the proteinase-catalyzed ester synthesis reaction with N-acetyl-L-tyrosine and ethanol. To guarantee the preservation of the enzyme activity and to allow for the extraction of the product in the organic phase, a biphasic system was used. The Vm increased for the modified enzyme. This phenomenon was linked to the modification of the protein as demonstrated by its chemical denaturation with sodium dodecyl sulfate.

Topics: Aldehydes; Amino Acids; Chemical Phenomena; Chemistry; Chymotrypsin; Kinetics; Protein Denaturation; Sodium Dodecyl Sulfate; Structure-Activity Relationship; Tyrosine

1987