Limited Proteolysis of the Bovine Pancreatic Secretory Trypsin Inhibitor at Acid pH
نویسندگان
چکیده
منابع مشابه
Limited proteolysis of the bovine pancreatic secretory trypsin inhibitor at acid pH.
The bovine pancreatic secretory trypsin inhibitor (Kazal’s inhibitor) undergoes a limited and specific proteolysis by catalytic amounts of trypsin in the presence of calcium ions at acidic pH. The pH optimum for both the initial rate of reaction and the extent of reaction is pH 2.7. Incubation of inhibitor with 0.7 mole % trypsin at pH 2.7 for 3 hours at 25” results in the modification of 25% o...
متن کاملExploring bovine pancreatic trypsin inhibitor phase transitions.
This paper presents an investigation of the phase diagram of BPTI (bovine pancreatic trypsin inhibitor)/350 mM KSCN at pH 4.9 by direct observation and numerical simulations. We report optical microscopy and light and X-ray scattering experiments coupled with theoretical data analysis using numerical tools. The phase diagram is thoroughly determined, as a function of temperature. Two polymorphs...
متن کاملTrypsin inhibitor from bovine pancreatic juice.
A trypsin inhibitor has been isolated in 54% yield from bovine pancreatic juice by gel filtration on Sephadex G-75 at pH 8.1 and by elution chromatography on DEAE-cellulose at pH 9.0. It appears to be homogeneous by equilibrium chromatography, equilibrium sedimentation ultracentrifugation, and amino acid analysis, and on the basis of the stoichiometry of its interaction with trypsin. The polype...
متن کاملDecamers observed in the crystals of bovine pancreatic trypsin inhibitor.
The structure of bovine pancreatic trypsin inhibitor (BPTI) has been solved at 2.1 A resolution in a new crystal form (space group P6422 with unit-cell dimensions a = b = 95.0, c = 158.1 A). The asymmetric unit is a pentamer, but a decamer is created by application of crystallographic symmetry. The decamer of BPTI is only the fourth such assembly reported to date in the Protein Data Bank.
متن کاملVarying occurrence of gastroduodenal immunoreactive pancreatic secretory trypsin inhibitor.
Operative specimens from various parts of gastroduodenal mucosa were analysed for immunoreactive pancreatic secretory trypsin inhibitor (PSTI) using a peroxidase-antiperoxidase method. Normal gastric mucosa exhibited a varying degree of PSTI immunoreactivity, which was more pronounced in the foveolar cells of gastric mucosa of fundus type than in the non-pepsinogen producing antrum-pyloric muco...
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: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)91968-x