What's the difference between pepsin and peptogenic?
Pepsin
Definition:
(n.) An unorganized proteolytic ferment or enzyme contained in the secretory glands of the stomach. In the gastric juice it is united with dilute hydrochloric acid (0.2 per cent, approximately) and the two together constitute the active portion of the digestive fluid. It is the active agent in the gastric juice of all animals.
Example Sentences:
(1) Accordingly, when bFGF, complexed to heparin, is treated with pepsin A, an aspartic protease with a broad specificity, only the Leu9-Pro10 peptide bond is cleaved generating the 146-amino acid form.
(2) Digestion is initiated in the gastric region by secretion of acid and pepsin; however, diversity of digestive enzymes is highest in the post-gastric alimentary canal with the greatest proteolytic activity in the spiral valve.
(3) The values obtained are shown to be lower than those calculated for arigid pepsin globule.
(4) This hydrostatic pressure may well be the driving force for creating channels for acid and pepsin to cross the mucus layer covering the mucosal surface.
(5) Binding activity was labile to heat, and to treatment with pepsin or trypsin.
(6) The molecular structure of the hexagonal crystal form of porcine pepsin (EC 3.4.23.1), an aspartic proteinase from the gastric mucosa, has been determined by molecular replacement using the fungal enzyme, penicillopepsin (EC 3.4.23.6), as the search model.
(7) Acid and pepsin output from the denervated pouch in response to pentagastrin and food decreased significantly (P less than 0.001) after parenteral feeding and returned to control levels after the dogs resumed a normal diet.
(8) Antigenic properties of crystalline pepsin, trypsin and chymotrypsin were studied in 9 rabbits immunised with these enzymes.
(9) The fibrosis of the gastric wall with motility disturbances, and the diminution of acid and pepsin production from damage to the glandular elements, would weigh against the addition of a vagotomy to the drainage procedure.
(10) The antigens were solubilized by treating the tissue samples with the proteolytic enzymes collagenase, trypsin and pepsin.
(11) Rates of digestion were in the order, pepsin approximately equal to trypsin much greater than papain.
(12) Urothelial cells were pepsin-extracted from paraffin-embedded specimens taken from human nontumorous bladder mucosa, dysplasia, and carcinoma in situ.
(13) Two main polypeptides, Mr about 27,000 and 21,000, were protected against pepsin proteolysis when a mixture consisting of asolectin vesicles and 125I-labeled tetanus toxin was subjected to a pH drop from 7.2 to 3.0.
(14) This suggests that its antiulcerogenic effect is due to decreases of acid and pepsin outputs which enhance gastric mucosal strength.
(15) The inhibition of pepsin-catalysed hydrolysis of N-acetyl-l-phenylalanyl-l-phenylalanylglycine by products and product analogues was studied.
(16) Small amounts of non-collagenous proteins and glycosaminoglycans of different compositions in dentin and bone resisted extraction before pepsin digestion.
(17) Each of the primary stress selected isolates was tested in synthetic saliva, rumen fluid simulating the activity in the rumen, rumen fluid followed by pepsin-hydrochloric acid treatment simulating the additional effect of ruminal and abomasal activity, pepsin-hydrochloric acid solution simulating conditions in the abomasum and finally in a trypsin solution as an example of enzyme activity in the gut.
(18) The predominant band in pepsin-treated tissues was 60-70 kDa, with additional forms of 250 and 150 kDa in neonatal heart and lung.
(19) Peptide 18 was rapidly cleaved by trypsin, but 19 was reasonably stable to all enzyme degradation systems tested with maximum degradation of 50% by pepsin in 3 h. Both 18 and 19 when given iv to normotensive rats were between 3 and 10 times more potent than captopril in inhibiting an angiotensin I induced blood pressure increase.
(20) Limited pepsin digestion of human plasma albumin at pH 3.5 and 0 degrees in the presence of octanoate caused cleavage at residue 307 of the albumin molecule to yield two fragments.