Studies on gastric proteolysis. 3. The secretion of different pepsins by fundic and pyloric glands of the stomach.
نویسنده
چکیده
It has been shown (Desreux & Herriott, 1939; Northrop, Kunitz & Herriott, 1948; Hoch, 1950; Merten, Schramm, Grassmann & Hannig, 1952; Taylor, 1956, 1959b) that crystalline swine pepsin contains more than one proteolytically active component. Merten et al. (1952) and Taylor (1959b) have also found more than one proteolytic component in pooled human gastric juice. The latter described two electrophoretically homogeneous components of human gastric juice which moved to the anode at pH 2-5 in the Tiselius apparatus and thus resembled pepsin. Each component digested serum albumin with two pH maxima, one near pH 2 and the other near pH 3.5. The origin of these active components of crystalline pepsin and gastric juice has not been satisfactorily settled. As Northrop et al. (1948) point out, crystalline pepsin from a single individual animal has never yet been isolated, so that different components may represent nothing more than pepsins from the different individuals who contributed to the original starting material. However, in the electrophoretic experiments mentioned above the gastric juice from which the two anodal-moving components were prepared was contributed by only two normal subjects; the pH maxima for digestion by the smaller component were at lower pH values than those of the larger, whereas the pH-activity curves of theoriginal juice of each subject showed maxima close to those of the larger component. It seemed therefore that the smaller component was not the main pepsin of either of the individuals but a substance with its activity masked in the original juices. This evidence suggests that there might be in each individual at least two pepsins, each exerting proteolytic action with two maxima below pH 5, but with definite differences in the pH values at which the maxima occur. A further clue to the origin of these components arose during the investigation of the proteolytic activity of extracts of gastric mucosa from different parts of the stomach (removed at operation) of patients with gastric or duodenal ulcer. Extracts of pyloric mucous membrane often gave
منابع مشابه
The pepsins from human gastric mucosal extracts.
1. The pepsins and pepsinogens of the gastric mucosal extracts of two normal subjects, of seven patients with gastric adenocarcinoma and of two patients with duodenal ulcer have been investigated by agar-gel electrophoresis and by ion-exchange chromatography. 2. Of the eight zones of proteolytic activity that have previously been reported in normal human gastric juice, seven can be detected in ...
متن کاملPeptic activity after the administration of Pentagastrin and in gastroduodenal disease.
The existence of more than one gastric pepsin has been reported by many authors. Herriott, Desreux, and Northrop (1940) separated two proteolytic fractions from human gastric juice by salt-fractionation methods, and similar results were described by Baker (1951) and Taylor (1959b). Using moving boundary electrophoresis, Kushner, Rapp, and Burtin (1964), Merten, Schramm, Grassmann, and Hannig (1...
متن کاملDistribution and relative frequency of immunohistochemically detected endocrine cells in the stomach of New Zealand White rabbit (Oryctolagus cuniculus)
Background: Gastrointestinal (GI) endocrine cells produce many GI hormones that perform various physiological functions of the digestive system. Aims: We aimed to investigate the presence and distribution of immunoreactive (IR) endocrine cells to glucagon, somatostatin, cholecystokinin-8 (CCK-8), serotonin, secretin and histamine in the stomach of adult male Ne...
متن کاملFormation constants for the complexes of adenosine di- or tri-phosphate with magnesium or calcium ions.
2. Swine pyloric juice also exhibited two proteolytic pH maxima, at pH values 1-6 and 2-6, which are lower than those of swine or human fundic extracts or of human gastric juice. 3. Crystalline swine pepsin can be separated into two components, one of which digested proteins with pH maxima close to those found with swine fundic mucosa and the other with maxima close to those found with pyloric ...
متن کاملDemonstration of chymosin (EC 3.4.23.4) in the stomach of newborn pig.
The stomach of newborn pig contains a proteinase that is immunologically closely related to calf chymosin (rennin) (EC 3.4.23.4.). None of the pepsins from the stomach of adult pig is present in the newborn pig. Pig chymosin has optimal general proteolytic activity around pH 3.5. The ratio of milk-clotting activity to general proteolytic activity is about 30--70 times higher than that of pylori...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Biochemical journal
دوره 71 2 شماره
صفحات -
تاریخ انتشار 1959