Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects have been examined of chymotrypsin, pepsin, trypsin, and pancreatic lipase on cattle rhodopsin in digitonin solution. The digestion of rhodopsin by chymotrypsin was measured by the hydrolysis of peptide bonds (formol titration), changes in pH, and bleaching. The digestion proceeds in two stages: an initial rapid hydrolysis which exposes about 30 amino groups per molecule, without bleaching; superimposed on a slower hydrolysis which exposes about 50 additional amino groups, with proportionate bleaching. The chymotryptic action begins at pH about 6.0 and increases logarithmically in rate to pH 9.2. Trypsin and pepsin also bleach rhodopsin in solution. A preparation of pancreatic lipase bleached it slightly, but no more than could be explained by contamination with proteases. In digitonin solution each rhodopsin molecule is associated in a micelle with about 200 molecules of digitonin; yet the latter do not appear to hinder enzyme action. It is suggested that the digitonin sheath is sufficiently fluid to be penetrated on collision with an enzyme molecule; and that once together the enzyme and substrate are held together by intermolecular attractive forces, and by the "cage effect" of bombardment by surrounding solvent molecules. The two stages of chymotryptic digestion of rhodopsin may correspond to an initial rapid fragmentation, such as has been observed with many proteinases and substrates; superimposed upon a slower digestion of the fragments. Since the first phase involves no bleaching, this may mean that rhodopsin can be broken into considerably smaller fragments without loss of optical properties.
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PMID:The action of enzymes on rhodopsin. 1358 19

EXPERIMENTS DESIGNED TO CHARACTERIZE AN UNIDENTIFIED TRANSMISSIBLE AGENT BROUGHT FORTH THE FOLLOWING FINDINGS: The cytopathology consisted of the formation of intranuclear globules, collapse of the involved nuclei, and the extrusion of nuclear materials. The relatively dormant primary human amnion cells were less susceptible than the rapidly growing cell lines. Similarly, the slowly multiplying ribose variants were less susceptible than their corresponding parent cell lines. Interferon-like activity was released from infected cells. Infectivity was readily demonstrated following storage at 0-4 degrees C for at least 8 months or at 37 degrees C for at least 2 weeks. Freeze-thawing, however, markedly reduced or completely destroyed its infectivity. Infectivity was destroyed completely by ether and chloroform; partially by desoxycholate, and not affected by trypsin, papain, RNAse, DNAse, hyaluronidase, lysozyme, lecithinase, or pancreatic lipase. The rate of inactivation by 0.025 per cent formalin was much slower than that of vaccinia and herpes viruses. Its synthesis was suppressed by 5-fluorodeoxyuridine. This suppression was not reversed by thymidine and/or uracil. Heat-stable neutralizing antibody could not be demonstrated in 379 human and animal serums, in human gamma globulins, or in serums from animals "immunized" with this agent. Heat-labile inhibitors (lipoprotein-like) capable of inhibiting the infectivity of this agent were demonstrated in 154 of the 157 serums tested. Experimental evidence indicated the non-identity of this ubiquitous inhibitor and the properdin system. The non-infectious complex between this agent and the ubiquitous serum inhibitor may be dissociated (hence, become infectious) by simple dilution. Repeated attempts to reisolate a similar agent have not been successful. We have hypothesized that this agent is a virus consisting of DNA wrapped in a surface coat rich in lipid, and suggest that this virus be referred to tentatively as a lipovirus.
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PMID:The biological, immunological, and physicochemical characterization of a transmissible agent capable of inducing DNA and thymine degradation in cultured human cells. 1387 2

After oral intake, small amounts of intact protein may be absorbed into the blood circulation. The current study investigated whether orally administered pancreatic enzymes were absorbed from the intestine. The study included 28 pigs; 3 control pigs with intact pancreatic function and 25 pigs that were made exocrine pancreas insufficient by duct ligation (20 pigs) or total pancreatectomy (5 pigs). The pigs received a pancreatic enzyme preparation (0, 2, 4, or 8 g of Creon 10,000) together with the feed. The blood plasma was analyzed for pancreatic lipase activity with a [3H]-triolein substrate assay, while (pro)colipase and cationic trypsin(ogen) levels were measured with enzyme-linked immunosorbent assay (ELISA). Administration of Creon (0-8 g) caused no significant changes in plasma (pro)colipase or cationic trypsin(ogen) levels. Lipase activity peaks in plasma samples were found, but they did not correspond to the administration of Creon. The potential source of these plasma lipase activity peaks is discussed. The results showed no absorption into blood of pancreatic enzymes after oral administration (0, 2, 4, or 8 g of Creon mixed with 100 g of feed) to pancreas-insufficient pigs.
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PMID:The enzyme levels in blood are not affected by oral administration of a pancreatic enzyme preparation (Creon 10,000) in pancreas-insufficient pigs. 1470 35

Purified lipase, injected intracerebrally and intravasculariy in rabbits, gave rise to focal areas of demyelinization in the central nervous system in 10 of 13 animals so treated. In one instance the lesions became manifest within 48 hours and in another they persisted for 6 months; they were not infrequently accompanied by paresis and by tilting or tremor of the head. They were characterized by a focal loss of myelin and moderate gliosis with little or no neuronal destruction or inflammatory reaction, in these respects resembling the plaques of multiple sclerosis. The intracerebral injection of trypsin and chymotrypsin in control animals failed to produce the characteristic demyelinization, but by contrast caused focal areas of necrosis in which all the cerebral tissues were involved. Furthermore, demyelinization did not result when heat-inactivated pancreatic lipase was injected intracerebrally, and similarly negative results were obtained when an incubated mixture comprised of fatty connective tissue that had been acted upon by the pancreatic preparation and then heated to inactivate the lipase, was injected into the brains of rabbits. In supplementary experiments the pancreatic lipase preparation and fresh rabbit brain, incubated together in vitro, were found to form acid, presumably owing to the breakdown of brain lipids to fatty acids; trypsin and chymotrypsin mixed with brain in control experiments failed to form acid. When incubated with segments of the spinal cord of experimental animals, the lipolytic enzyme brought about a loss of stainable myelin in peripheral areas and in the spinal nerve roots; again trypsin and chymotrypsin had no such effect in control experiments. The findings as a whole show that an enzyme preparation with lipolytic activity has the ability to destroy myelin in living animals, and in vitro as well, and to produce lesions remarkably similar to those of multiple sclerosis. They have additional interest in light of the demonstration that a lipolytic enzyme is regularly present in the reactive histiocytes of guinea pigs with experimental encephalomyelitis (5).
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PMID:Demyelinization induced in living rabbits by means of a lipolytic enzyme preparation. 1482 2

In humans, pancreatic hyperechogenicity and duct dilation are reported as normal aging changes. Similar changes have been reported with pancreatitis in the cat. We attempted to determine if aging changes occur in the ultrasound appearance of the normal feline pancreas. The pancreas of 84 normal (based on history, physical exam, biochemical profile, and feline trypsin-like immunoreactivity and pancreatic lipase immunoreactivity concentrations) cats of varying ages was scanned. Pancreatic width at the left limb and body, pancreatic duct diameter at left limb and body, and pancreatic echogenicity compared with liver and surrounding fat were noted and compared with age and body weight. Lower and upper limits of the 95% reference intervals for pancreatic left limb width were 2.6 and 9.5 mm, and 3.5 and 8.5 mm for the pancreatic body width. There was no significant difference in pancreatic width between the left limb and body. Lower and upper limits of the 95% reference interval for the diameter of the pancreatic duct at the left limb and body were similar, and were 0.65 and 2.5 mm. There was a weak but significant linear correlation between pancreatic duct diameter and age, with increasing pancreatic duct diameter with increasing age. There was no correlation of pancreatic width with age, and no correlation of pancreatic echogenicity with age or body weight. Based on this study, feline pancreatic size and echogenicity do not change with age. Pancreatic duct diameter increases slightly with age and should not be used as a sole indicator of pancreatitis in the geriatric cat.
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PMID:Age-relatedchanges in the ultrasound appearance of the normal feline pancreas. 1605 Feb 83

The state of chlorophyll in chloroplast fragments is affected by such factors as the ionic strength and pH of the suspending medium. With increasing ionic strength or at pH values other than neutrality, there is a decrease in the fluorescence yield of the form of chlorophyll with fluorescence maximum at 715 to 736 mmu (aggregate) and an increase in the yield of the form with fluorescence maximum at 685 mmu (monomer). (Positions of maxima cited are for 77 degrees K.) These changes in yield are accompanied by modifications in absorption and fluorescence excitation spectra. It is also noted that these effects are similar to the ones brought about by pancreatic lipase, wheat germ lipase, pancreatic trypsin or urea. An interpretation is given which is consistent with the experimental data, namely, that the effects originate in conformational changes in the proteins to which the pigments are attached. These conformational changes give rise to an increase in the size of the aggregate and a decrease in the probability of energy transfer between the monomer and aggregates.
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PMID:Effect of method of preparation on the States of chlorophyll in euglena chloroplast fragments as determined by fluorescence spectroscopy. 1665 62

Digestion of spinach chloroplasts with pancreatic lipase or trypsin effectively uncoupled electron transport. Continued digestion led to inhibition of saturated rates of Hill reaction activity and a decrease in quantum yield. Irradiation with ultraviolet light decreased the quantum yield and inhibited Hill activity, but did not uncouple. Ascorbate-dichlorophenol-indophenol-mediated reduction of nicotinamide adenine dinucleotide phosphate was not appreciably inhibited by treatment with either of the enzymes or by ultraviolet irradiation.Carbonylcyanide m-chlorophenylhydrazone became a potent inhibitor of electron transport after trypsin treatment of chloroplasts. It also inhibited, rather than uncoupled, electron transport in glutaraldehyde-fixed chloroplasts. No other uncouplers tested showed these effects. Glutaraldehyde fixation of chloroplasts also greatly reduced the inhibitory effects of lipase and trypsin digestion but not the inhibition by ultraviolet irradiation.The inhibitory effects of trypsin and pancreatic lipase, and probably ultraviolet irradiation as well, appear to be due to a general breakdown of the membrane structure rather than inactivation of specific sites in the electron transport chain.
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PMID:Some effects of hydrolytic enzymes on coupled and uncoupled electron flow in chloroplasts. 1665 42

Three colipases were purified from pancreas of two birds (ostrich and turkey) and one mammal (dromedary). After acidic and/or heat treatment and precipitation by sulfate ammonium and then ethanol, cofactors were purified by Sephadex G-50 gel filtration followed by ion-exchange chromatography first on Mono S and then on Mono Q. One molecular form was obtained from each species with a molecular mass of approximately 10 kDa. Cofactors were not glycosylated. The N-terminal sequences of the three purified cofactors showed high sequence homology. A 90 amino acid sequence of the ostrich cofactor was established based on peptide sequences from four different digests of the denaturated protein using trypsin, chymotrypsin, thermolysin, or staphylococcal protease. This sequence exhibited a high degree of homology with chicken and mammal cofactors. Bile salt-inhibited pancreatic lipases from five species were activated to variable extents by colipases from bird and mammal origins. The bird pancreatic lipase-colipase system appears to be functionally similar to homologous lipolytic systems from higher mammals. Our comparative study showed that mammal colipase presents a lower activation level toward bird lipases than the bird counterpart. Three-dimensional modeling of ostrich colipase suggested a structural explanation of this fact.
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PMID:Biochemical and structural comparative study between bird and mammal pancreatic colipases. 1695 80

Hormone-sensitive lipase (HSL) contributes importantly to the mobilization of fatty acids from the triacylglycerols stored in adipocytes, which provide the main source of energy in mammals. On the basis of amino acid sequence alignments and three-dimensional structures, this enzyme was previously found to be a suitable template for defining a family of serine carboxylester hydrolases. In this study, the HSL family members are characterized rather on the basis of their inhibition by 5-methoxy-3-(4-phenoxyphenyl)-3H-[1,3,4]oxadiazol-2-one (compound 7600). This compound inhibits mammalian HSL as well as other HSL family members, such as EST2 from the thermophilic eubacterium Alicyclobacillus acidocaldarius and AFEST from the hyperthermophilic archaeon Archaeoglobus fulgidus. Various carboxylester hydrolases that are not members of the HSL family were found not to be inhibited by compound 7600 under the same experimental conditions. These include nonlipolytic hydrolases such as Torpedo californica acetylcholinesterase and pig liver esterase, as well as lipolytic hydrolases such as human pancreatic lipase, dog gastric lipase, Thermomyces lanuginosus lipase, and Bacillus subtilis LipA. When vinyl esters were used as substrates, the residual activity of HSL, AFEST, and EST2 decreased with an increase in compound 7600 concentration in the incubation mixture. The inhibitor concentration at which the enzyme activity decreased to 50% after incubation for 5 min was 70, 20, and 15 nM with HSL, AFEST, and EST2, respectively. Treating EST2 and AFEST with the inhibitor resulted in an increase in the molecular mass, as established by performing matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis. This increase in the molecular mass, which corresponds approximately to the molecular mass of the inhibitor, indicates that a covalent enzyme-inhibitor complex has been formed. Surface-enhanced laser desorption ionization time-of-flight mass spectrometry analysis of a trypsin digest of AFEST treated with the inhibitor or not treated showed the occurrence of an increase in the molecular masses of the "GESAGG"-containing peptide, which is compatible with the formation of a covalent complex with the inhibitor.
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PMID:Use of an inhibitor to identify members of the hormone-sensitive lipase family. 1711 13

Pancreatitis is the most common disorder of the exocrine pancreas in cats and is clinically important in this species. Despite that fact, the pathophysiology of feline pancreatitis is poorly understood, and its etiology remains unknown in the majority of cases. Arriving at a clinical diagnosis of feline pancreatitis remains challenging because cats with pancreatitis exhibit mild and nonspecific clinical signs, which account for the low level of suspicion for this disease by veterinary clinicians. In addition, sensitive and specific tests for the diagnosis of feline pancreatitis were, until recently, not available. Suspicion of pancreatitis should be based on a detailed history and physical examination, hematologic, clinicopathologic, and imaging findings. A diagnosis of feline pancreatitis should be confirmed by measurement of feline pancreatic lipase immunoreactivity, abdominal ultrasound, pancreatic cytology, and/or pancreatic histopathology. Serum amylase and lipase concentrations are of no value, whereas feline trypsin-like immunoreactivity concentrations are of limited value for the diagnosis of feline pancreatitis. Abdominal ultrasound may be useful but requires experience, and normal findings do not exclude pancreatitis. Management of pancreatitis is based on supportive therapy and dietary measures. Finally, management of complications and/or concurrent diseases is also crucial in cats with pancreatitis.
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PMID:Current concepts in feline pancreatitis. 1908 52


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