scholarly journals Studies on Soybean Trypsin Inhibitors. 2. Amino-Acid Sequence around the Reactive Site of Soybean Trypsin Inhibitor (Kunitz)

1973 ◽  
Vol 32 (3) ◽  
pp. 408-416 ◽  
Author(s):  
Takehiko Koide ◽  
Tokuji IKENAKA ◽  
Susumu Tsunasawa
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Trypsin Inhibitor ◽  
Trypsin Inhibitors ◽  
Soybean Trypsin Inhibitor ◽  
Reactive Site

The amino acid sequence and reactive site of a single-headed trypsin inhibitor from wheat endosperm

1994 ◽  
Vol 13 (2) ◽  
pp. 187-194 ◽  
Author(s):  
Elia Poerio ◽  
Carlo Caporale ◽  
Lucia Carrano ◽  
Carla Caruso ◽  
Francesco Vacca ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Trypsin Inhibitor ◽  
Reactive Site ◽  
Wheat Endosperm

Partial Sequence of Trypsin Inhibitor From Ovomucoid

1973 ◽  
Vol 51 (11) ◽  
pp. 1548-1551 ◽  
Author(s):  
G. S. Murthy ◽  
C. Gilardeau ◽  
M. Chrétien
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Trypsin Inhibitor ◽  
Trypsin Inhibitors ◽  
Terminal Region ◽  
The Other ◽  
Partial Sequence ◽  
Amino Acid Residues

The amino acid sequence of the 40 amino acid residues at the N-terminal region of trypsin inhibitor from chick ovomucoid has been determined. This part of the sequence does not show any homology with any region of the other known trypsin inhibitors.

scholarly journals Antiproteolytic activity of goose pancreas: purification, inhibitory properties and amino-acid sequence of a Kazal type trypsin inhibitor.

1996 ◽  
Vol 43 (3) ◽  
pp. 489-496 ◽  
Author(s):  
A Wilimowska-Pelc ◽  
D Stachowiak ◽  
M Gładysz ◽  
Z Olichwier ◽  
A Polanowski
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Trypsin Inhibitor ◽  
Association Constant ◽  
Amino Acid Residues ◽  
High Homology ◽  
Reactive Site ◽  
Reverse Phase Hplc ◽  
Reverse Phase ◽  
Antiproteolytic Activity

A trypsin inhibitor of Kazal type has been isolated from goose pancreas by affinity chromatography on immobilized anhydrotrypsin, anion exchange and reverse phase HPLC. It inhibits bovine beta-trypsin with the association constant (Ka) of 5.99 x 10(8) M-1. The complete amino-acid sequence was determined following CNBr treatment. The protein comprised a total of 69 amino-acid residues, corresponding to a molecular mass of 7.7 kDa. The P1-P'1 reactive site bond of the inhibitor was localized at position Lys25-Met26. The amino-acid sequence of GPTI shows extremely high homology to that of other inhibitors isolated from pancreas of birds.

Sign in / Sign up

Export Citation Format

Share Document