SPECIFICITY OF CHYMOTRYPSIN B
نویسندگان
چکیده
منابع مشابه
Specificity of chymotrypsin B.
Brown, Shupe, and Laskowski (1) have described the isolation, from beef pancreas, of a crystalline proteolytic enzyme which they have named “activated protein B” or “chymotrypsin B.” Through the kindness of Dr. Laskowski who provided us with a 4 times recrystallized sample of this enzyme, it was possible to examine its action on a series of synthetic peptides and peptide derivatives. The data p...
متن کاملCrystalline activated protein B (chymotrypsin B).
The protein isolated from beef pancreas (1) was recently identified as the zymogen of a proteolytic enzyme and provisionally called protein B (2). In this paper a method of crystallization of the activated enzyme is described. Further properties of this enzyme have been studied, suggesting that the activated protein B belongs to the group of chymotrypsins. The strongest evidence for this conclu...
متن کاملA change in specificity of chymotrypsin caused by chemical modification of methionine residues.
The specificity patterns of chymotrypsins in which the methionine residues have been converted to the sulfoxide have been examined relative to the native enzyme. When the surface methionine residue 3 residues away from the active serine is oxidized, the specificity pattern is quite similar to the native enzyme as judged by the relative rates of hydrolysis of ester and peptide substrates. When b...
متن کاملFunctional characterization of the cleavage specificity of the sapovirus chymotrypsin-like protease.
Sapovirus is a positive-stranded RNA virus with a translational strategy based on processing of a polyprotein precursor by a chymotrypsin-like protease. So far, the molecular mechanisms regulating cleavage specificity of the viral protease are poorly understood. In this study, the catalytic activities and substrate specificities of the predicted forms of the viral protease, the 3C-like protease...
متن کاملSpecificity of trypsin and chymotrypsin: loop-motion-controlled dynamic correlation as a determinant.
Trypsin and chymotrypsin are both serine proteases with high sequence and structural similarities, but with different substrate specificity. Previous experiments have demonstrated the critical role of the two loops outside the binding pocket in controlling the specificity of the two enzymes. To understand the mechanism of such a control of specificity by distant loops, we have used the Gaussian...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1948
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)35560-1