Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The C-terminal region-sepcific anti-glucagon sera were raised in rabbits using as immunogen, and conjugate of BSA and a C-terminal fragment of pancreatic glucagon. The hapten was prepared by trypsin digestion of the glucagon, which was proved to be a 1:3 mixture of glucagon (18--29) and (19--29). Six rabbits were immunized by subcutaneous injection of an emulsion of the conjugate with complete Freund's adjuvant and five of the rabbits produced antibodies to the glucagon (GC-1, GC-2, GC-3, GC-5 and GC-6). For comparison, rabbit antisera were also produced against glucagon polymer (GA-10) and syrupy glucagon fibrils (PGA-2). All these antisera as well as the pancreatic glucagon-specific antiserum 30 K were characterized with dog gut-extract (gut-GLI) and glucagon-related peptide fragments in the radioimmunoassay systems. The assay systems utilized 125 I-monosubstituted pancreatic glucagon as tracer and human mono-component glucagon as standard. All sera of the GC-series crossreacted with the dog gut-extract very weakly and antisera GC-5 and GC-6 exhibited the lowest crossreactivities with the extract, which were shown to be as low as that of 30k. Characterization of the antiserum GC-5 with purified glucagon related fragments indicated that the major antigenic determinant located exactly in the C-terminal region of glucagon. The present results clearly showed high efficiency of the use of the glucagon C-terminal fragment as hepatenic immunogen in obtaining the C-terminal region-specific, i.e., pancreatic glucagon-specific antisera.
 ...
PMID:Production of anti-glucagon sera with a C-terminal fragment of pancreatic glucagon. 8 40

By means of the indirect immunofluorescence and immunenzyme technique trypsin and trypsin-like activity in fixed cryostate sections of pancreas and gut and pellets of isolated pancreatic islets respectively were investigated using specific antiserum against trypsin. The enzyme was demonstrated in the cytoplasma of the acinus cells, the epithel cell of the intercalated ducts and the excretory (interlobular) ducts of the exocrine pancreas. By light and fluorescence microscopy we could also localize a high activity in pancreatic islets. Results taken from electron microscope show the enzyme in the region of the peripheral endoplasmatic reticulum, the surface of the mitochondria, the zymogen granules of the acinus cells and in the region of the membranes of the endoplasmatic reticulum and in the granules of the B-cells of the pancreatic islets. These results are discussed in correlation with biochemical data concerning the importance of trypsin/trypsin-like activity in the specific conversion of prohormones into hormones.
 ...
PMID:[The immunhistochemical investigation of trypsin and trypsin-like-activity in the small intestine, pancreas and isolated Langerhans islets. A light-, fluorescent- and electron microscopic study (author's transl)]. 10 56

Both immunoreactive intact cholecystokinin (CCK33) and its COOH-terminal octapeptide (CCK8) are detected in brain and gut extracts of monkey, dog, and pig using an antiserum with equivalent sensitivities for detecting CCK8 in the free form or when incorporated in the intact molecule. The failure to detect intact cholecystokinin in extracts from monkey or dog by using an antiserum developed by immunization with porcine CCK33 is due to marked species differences in the NH2-terminal portion of the molecule. Immunohistochemical staining reveals the presence of CCK peptides in rabbit cerebral cortical tissue neurons. Subcellular fractionation of rat cerebral cortical tissue demonstrates that CCK immunoreactivity is concentrated in the pellet identified by electron microscopy to contain a high proportion of synaptic vesicles. A converting enzyme that differs from trypsin has been partially purified from canine and porcine cerebral cortical extracts. It converts porcine CCK to smaller immunoreactive forms, but fails to convert big gastrin to heptadecapeptide gastrin. This enzyme differs from trypsin not only in substrate specificity but also in several physicochemical properties. Cerebral cortical extracts from hyperphagic ob/ob mice have strikingly lower contents of CCK than those from their lean littermates and other normal mice. These studies taken together are consistent with a role for CCK as a neurotransmitter involved in the overall regulation of appetite.
 ...
PMID:Gastrointestinal peptides in the brain. 11 Jun 22

Culture filtrates of enteropathogenic strains of E. coli from adult patients with cholera-like diarrhoea produced a rhythm-disturbing effect when injected into isolated sacklets of rabbit ileum. This action was shown to be medium-dependant. It could not be elicited by cultures grown in synthetic medium. Meat extract cultures gave variable results, but the gut movements could be irritated regularly when cultures were grown in a casamino acids - yeast extract medium (table, figure). This activity which was not associated with non-pathogenic strains appeared in the beginning of the stationary phase of growth. The factor responsible for the dysrhythmic effect could be precipitated by ammonium sulphate, was dialysable, withstood boiling for 10 minutes (figure) and treatment with trypsin, chymotrypsin and pancreatin. Antisera prepared against culture filtrates of strain 10407 containing agglutinating and vascular permeability neutralizing antibodies did not neutralize the gut irritating effect efficiently. We conclude that the factor of our assay system is perhaps closely related to the heat-stable enterotoxin described by other authors concerned by E. coli enterotoxins.
 ...
PMID:[Toxin production by enteropathogenic colibacilli in adult persons (author's transl)]. 24 Nov 79

An enzyme has been partially purified from canine and porcine cerebral cortical extracts that differs from trypsin in that it manifests some degree of hormone specificity since it converts porcine cholecystokinin to smaller immunoreactive forms, i.e., the COOH-terminal dodecapeptide and octapeptide fragments, but fails to convert big gastrin (34 amino acids) to heptadecapeptide gastrin. This enzyme is distinguishable from trypsin not only in substrate specificity, but also in several physiochemical properties. It is not inhibited in the presence of concentrations of lima bean trypsin inhibitor sufficient to inhibit 1 mg of trypsin per ml of incubation mixture. It is inactivated when incubated with substrate at 45 degrees C for 1 hr, whereas trypsin remains fully active when incubated under the same conditions at 55 degrees C. The enzyme elutes in the void volume on Sephadex G-50 and G-75 gel filtration. On sucrose gradient centrifugation, the proteolytic activity associated with trypsin is recovered above albumin but that of the solubilized brain enzyme is recovered below gamma globulin. The enzyme is not detectable in splenic extracts, which do contain nonspecific proteases capable of completely degrading cholecystokinin. Further investigation is required to determine whether the enzyme in the gut that converts cholecystokinin to the bioactive and immunoactive COOH-terminal fragments resembles or is different from the brain converting enzyme.
 ...
PMID:Characterization of a nontrypsin cholecystokinin converting enzyme in mammalian brain. 28 18

Crude preparations of hog gastric intrinsic factor or their own previously collected gastric juices administered with labeled vitamin B12 did not enhance vitamin B12 absorption in patients with vitamin B12 malabsorption secondary to pancreatic insufficiency. However, when these sources of gastric intrinsic factor were incubated with three times crystallized preparations of insolubilized bovine trypsin or chymotrypsin, the proteolytic enzymes were removed by centrifugation, and the preparations of gastric intrinsic factor were readministered to these patients, the absorption of vitamin B12 was markedly enhanced. Studies of hog gastric intrinsic factor before and after exposure to proteolytic enzymes failed to show any difference on Sephadex chromatography or polyacrylamide gel electrophoresis or on its affinity for vitamin B12 or the ileal receptor in guinea pigs. These investigations demonstrate that: (1) gastric intrinsic factor as secreted by subjects with pancreatic insufficiency or obtained from hog pyloric mucosal extracts is ineffective in promoting vitamin B12 absorption in patients with pancreatic insufficiency, (2) incubation of crude preparations of gastric intrinsic factor with insolubilized pancreatic proteases modified these preparations of gastric intrinsic factor in an as yet undefined manner, allowing them to enhance vitamin B12 absorption, and (3) in vitro studies using gut sacs or brush border preparations do not reflect the abnormality in vitamin B12 absorption associated with pancreatic dysfunction.
 ...
PMID:Evidence that pancreatic proteases enhance vitamin B12 absorption by acting on curde preparations of hog gastric intrinsic factor and human gastric juice. 31 82

To investigate further the cause of the pancreatic enlargment induced by orally ingested soybean trypsin inhibitor (STI), antibodies raised against STI and purified by affinity chromatography were used to localise dietary STI in the rat gut by fluorescent immunocytochemical methods. This technique permitted the clear intracellular demonstration of STI in the ileal mucosa of suckling rats. However, in adult rats no entry of STI into mucosal cells of the small intestine could be demonstrated, it being confined to the luminal surface of the mucosa. Although the passage of STI into and across the adult intestinal mucosa could not be excluded through the use of this technique, the results are consistent with an intraluminal mode of action of STI as suggested by Green and Lyman (1972)--namely, that the pancreatic enlargement caused in sensitive species results from the inhibition of trypsin (which acts as the physiological inhibitor of the mucosal secretion of pancreotrophic hormones), thus resulting in the uninhibited secretion of these hormones.
 ...
PMID:Immunocytochemical study of the interaction of soybean trypsin inhibitor with rat intestinal mucosa. 34 80

1. The food intake, pancreas weight and trypsin (EC 3.4.21.4) and alpha-chymotrypsin (EC 3.4.21.1) activities in the pancreas were measured in rats during pregnancy and lactation and after the young were weaned. 2. All the quantities measured increased significantly during lactation and had returned to their original values by 4 weeks after weaning. Food intake and pancreas weight were highest after the second week of lactation. Total trypsin and alpha-chymotrypsin activity, and the activity per g tissue, fell during pregnancy and rose during lactation, reaching a maximum 1 week after weaning. 3. From these and other results it is suggested that the hypertrophy and hypersecretion of pregnancy and lactation are initiated by changes insulin secretion and mediated by the trophic effects of gut hormones, and that differences in the nature and timing of the response may be controlled by nutrient availability.
 ...
PMID:The effects of pregnancy and lactation on the activities of trypsin and alpha-chymotrypsin in the rat pancreas. 46 45

Protein digestion and absorption was studied in rats with 6-week-old surgically constructed self-filling intestinal blind loops and steatorrhea, ie, blind-loop animals and controls were fed a 14C-labeled protein meal containing a nonabsorbable marker, 51CrCl3, and sacrificed 1 or 2 hr later. Intestinal contents were analyzed for 14C, 51Cr, protein, trypsin, and the products of digestion. At 1 hr, 14C absorption was greater in controls, but at 2 hr there was no difference in absorption between the two groups. Marker studies showed that blind-loop filling resulted in a delay of the progression of intestinal contents distally. Intraluminal trypsin and porteolysis were similar in the two groups. Endogenous protein was greater in the blind-loop animals. The early stages of the blind-loop syndrome may be characterized by delayed protein absorption secondary to blind-loop filling, which is compensated for by the distal gut resulting in an absence of overall protein malabsorption.
 ...
PMID:Protein digestion and absorption in the blind loop syndrome. 51 93

The digestion and absorption of collagen, native and artificially cross-linked, has been examined in the rat and the Gaboon viper, by feeding known quantities and measuring the hydroxy-proline content of the faeces and of the contents of the gut at different levels, and comparing with an unabsorbable marker (polyethylene glycol). Incubation of collagen in vitro with pepsin at 37 degrees C at pH 1.5 followed by trypsin or chymotrypsin converted about 40% into dialysable material.
 ...
PMID:Digestion of native collagen in the gut. 63 45


1 2 3 4 5 6 7 8 9 10 Next >>