TY - JOUR
T1 - The denaturation of trypsin
AU - Wu, Hua Lin
AU - Kundrot, Craig
AU - Bender, Myron L.
PY - 1982/7/30
Y1 - 1982/7/30
N2 - The denaturation of α- and β-trypsin in alkaline and neutral solution was studied. The denaturation of α-trypsin was a strict second-order reaction at neutrality. However, the denaturation of β-trypsin was not a pure secondorder reaction at the same pH. Calcium ion retarded the rate of β-trypsin denaturation to a greater extent than that of α-trypsin. In alkaline solution, trypsin has very short half life (t case1 2 < 30 minutes). On the other hand, the denaturation of immobilized trypsin in alkaline solution is a first-order reaction as is immobilized chymotrypsin. The rates of these two denaturations are similar. Calcium ion does not affect the rate of trypsin denaturation in alkaline solution.
AB - The denaturation of α- and β-trypsin in alkaline and neutral solution was studied. The denaturation of α-trypsin was a strict second-order reaction at neutrality. However, the denaturation of β-trypsin was not a pure secondorder reaction at the same pH. Calcium ion retarded the rate of β-trypsin denaturation to a greater extent than that of α-trypsin. In alkaline solution, trypsin has very short half life (t case1 2 < 30 minutes). On the other hand, the denaturation of immobilized trypsin in alkaline solution is a first-order reaction as is immobilized chymotrypsin. The rates of these two denaturations are similar. Calcium ion does not affect the rate of trypsin denaturation in alkaline solution.
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U2 - 10.1016/0006-291X(82)91553-4
DO - 10.1016/0006-291X(82)91553-4
M3 - Article
C2 - 7126237
AN - SCOPUS:0020493889
SN - 0006-291X
VL - 107
SP - 742
EP - 745
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -