Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
Annals of the New York Academy of Sciences
140 (1967), S. 0
ISSN:
1749-6632
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Natural Sciences in General
Notes:
Human gastric juice contains at least three different proteases which have been separated by column chromatography. Gastricsin is most probably one of these separated by this method. Proteolytic activity occurs over a pH range of approximately 0.5 to 4.0 in this composite protease mixture. Separation of the activities of individual proteases in gastric juice by simple pH control is not possible by current methods. Individual substrate differences may eventually lead to relatively simple methods of separation. Our usual laboratory procedures provide a partial summation of total gastric protease activity.The radioactive iodinated albumin method for protease measurements is a satisfactory and relatively simple laboratory procedure that can be applied to undiluted gastric juice. Results are related to a standard of purified pepsin of known specific activity and can therefore be reported in pepsin units.Clinical application of this method demonstrates that (1) protease is always present when acid is present; (2) Histalog stimulates the release of protease; (3) anticholinergic drugs may sometimes block the release of free acid but not protease; and (4) selective alteration of acid and protease appears to depend upon the intensity of pharmacologic stimulation or blockade of the vagus nerve.Clinical application of this method demonstrates that synthetic sulfated amylopectin has significant antipeptic activity both in vitro and in vivo.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1749-6632.1967.tb50995.x
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