C. Gray, S. Jonas
Oct 1, 1986
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Influential Citations
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Journal
International Journal of Biological Macromolecules
Abstract
Abstract The preparation is reported of p-azidosulphonyl-N′-butylbenzamide (ASBB). This was produced by the reaction of 1 molar equivalent of butylamine with p-azidosulphonylbenzoyl azide. ASBB reacted with butylamine to give -N-butylaminosulphonyl-N′-butylbenzamide, and with proteins, modifying them at their lysyl residues. ASBB reduced the number of ninhydrin-detectable amino groups in β- d -glucosidase by 25%, in trypsin by 44% and in chymotrypsin by 25%. In water, ASBB-modified trypsin was more stable than the native enzyme, although in 20% dioxane-water, in which native trypsin shows considerable stability, the modified enzyme was less stable than the native form. ASBB-modified chymotrypsin was not significantly more stable than chymotrypsin itself.