منابع مشابه
Studies on the Active Site of Chymotrypsin.
as it rises in b to enter c above the midline, etc. It can be easily seen that a similar oscillation about the midline takes place in the rotating fluid annulus of Figure 4a and in the more general situation of Figure 4b. These oscillations can be made quite small by adjusting the density of the buffer to match the particle density and by speeding up the rate of buffer flow to shorten the perio...
متن کاملActive Site of alpha-Chymotrypsin Activation by Association-Desolvation.
High reactivity toward alpha-chymotrypsin is observed for derivatives of beta-arylpropionic acids of varied structure-L-alpha-acylamido compounds, D-cyclized compounds, and, now, L-glycolamide esters. Compensating enthalpy and entropy effects are observed which appear to be caused by changes in water of solvation. High reactivity with varied structure, and physical evidence, appear to rule out ...
متن کاملPreferential Oxidation of the Methionine Residue near the Active Site of Chymotrypsin.
Hartley (4) has reported the amino acid sequence of a 25-residue peptide from the tryptic digest of X-sulfochymotrypsinogen which contains the “active center” serine as well as both methionine residues of a-chymotrypsin (Fig. 1). By kinetic analysis, Ray et al. (5, 6) deduced that 1 of the 2 methionine residues and 1 of the 2 histidine residues in chymotrypsin are rapidly destroyed on photo-oxi...
متن کاملThe Specific Binding of Biebrich Scarlet to the Active Site of a-Chymotrypsin*
This paper reports on the presence of a strong binding site for the dye Biebrich Scarlet, (6-[Z-hydroxy-l-naphthyl]azo)3,4’-azodibenzene sulfonic acid, on cr-chymotrypsin. The 1: 1 protein-dye complex is characterized by a Kdiss of 8.8 f 0.1 X 10U5 M in 0.1 M phosphate buffer at pH 7.6 and W’. Complex formation is associated with a red shift in the visible spectrum of the dye, and a characteris...
متن کاملThe Specific Binding of Biebrich Scarlet to the Active Site of a-Chymotrypsin*
This paper reports on the presence of a strong binding site for the dye Biebrich Scarlet, (6-[Z-hydroxy-l-naphthyl]azo)3,4’-azodibenzene sulfonic acid, on cr-chymotrypsin. The 1: 1 protein-dye complex is characterized by a Kdiss of 8.8 f 0.1 X 10U5 M in 0.1 M phosphate buffer at pH 7.6 and W’. Complex formation is associated with a red shift in the visible spectrum of the dye, and a characteris...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)93416-2