منابع مشابه
Release and recovery of porcine pepsin and bovine chymosin from reverse micelles: a new technique based on isopropyl alcohol addition.
After complete solubilization by the direct method, porcine pepsin was not released from AOT in isooctane reverse micelles even under aqueous-phase conditions which would not ordinarily allow uptake. Similarly, bovine chymosin, once forward-transferred at a pH below its isoelectric point, was not back-transferred into an aqueous contact phase buffered at a pH value above its isoelectric point. ...
متن کاملFeatures of the acid protease partition in aqueous two-phase systems of polyethylene glycol-phosphate: chymosin and pepsin.
The partitioning of chymosin (from Aspergilus niger) and pepsin (from bovine stomach) was carried out in aqueous-two phase systems formed by polyethyleneglycol-potassium phosphate. The effects of polymer concentration, molecular mass and temperature were analysed. The partition was assayed at pH 7.0 in systems of polyethyleneglycol of molecular mass: 1450, 3350, 6000 and 8000. Both proteins sho...
متن کاملThe primary structure of calf chymosin.
The complete amino acid sequence of calf chymosin (rennin) (EC 3.4.23.4) has been determined. The sequence consists of a single peptide chain of 323 amino acid residues. The primary structure of the precursor part of calf prochymosin was published previously (Pedersen, V.B., and Foltmann, B. (1975) Eur. J. Biochem. 55, 95-103), thus we are now able to account for the total 365 amino acid residu...
متن کاملCrystalline Pepsin
The decrease in protein nitrogen and in the activity of solutions of crystalline pepsin at pH 1.8 and 45 degrees C. has been determined. The decrease in activity, as measured with eleven different methods, is in exact proportion to the decrease of protein nitrogen of the solution. The measurements were continued until less than 5 per cent of the original protein remained. These results indicate...
متن کاملCrystalline Pepsin Iii. Preparation of Active Crystalline Pepsin from Inactive Denatured Pepsin By
The results (1) of the experiments with crystalline pepsin isolated from crude pepsin preparations indicated that the material is a pure substance and that the proteolytic activity is a property of the protein molecule itself and is not due to the presence of a separate non-protein impurity. No indication of the presence of a more highly active nonprotein molecule was obtained in the solubility...
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ژورنال
عنوان ژورنال: Hoppe-Seyler´s Zeitschrift für physiologische Chemie
سال: 1908
ISSN: 0018-4888
DOI: 10.1515/bchm2.1908.54.1.32