PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “PEPTIDE HYDROLASES”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 145 records · Page 8Linked to original sources
PubMed1984

Comparisons of Peptide hydrolase activities in cereals.

Carboxypeptidase activity (hydrolysis of N-carbobenzoxy-l-phenylalanyl-l-alanine) is high in a number of temperate zone cereals, originating in Asia Minor (wheat, barley, oats, wild oats, rye, triticale) compared to other cereals originating in central America or Asia (maize, sorghum, rice). However, endopeptidase activity (hydrolysis of azocasein or hemoglobin) is relatively much higher in the latter group. Comparison of trichloroacetic acid (TCA)-soluble products derived from the hydrolysis of hemoglobin showed that carboxyterminal amino acids (histidine, arginine, and tyrosine), are released when extracts from wheat and barley endosperms are used. With extracts from corn endosperms, much more TCA-soluble ultraviolet- absorbing material is released, but very little is released as free amino acids within the first 2 hours and the expected C-terminal amino acids of hemoglobin are not detected in significant amounts. These results suggest that the method of hydrolysis of the storage proteins may be significantly different in these two classes of cereals.

Journal Article↗
PubMed1983

A kininase and a kinin-converting enzyme: two distinct alpha aminoacyl peptide hydrolases from bovine lung.

Two closely related but different aminopeptidases from bovine lung have been isolated and characterized. The first aminopeptidase, which removes the N-terminal arginine residue from L-arginyl-L-prolyl-L-proline, bradykinin, and des-[Arg9]-bradykinin, has kininase activity; it has a pH optimum of 8.0, is stimulated by Mn2+, and its molecular weight in dilute buffers is slightly greater than 240,000 daltons. The second aminopeptidase, which converts kallidin to bradykinin, has kinin-converting activity; it has a pH optimum of 6.8, is stimulated by Co2+, and its molecular weight in dilute buffers is 250,000 daltons. The kinin-converting enzyme is blocked from action when the N-terminal penultimate residue is proline.

Aminopeptidases↗
PubMed1982

[The intestinal phase of peptide absorption].

Peptides and not amino acids are the prevailing degradation products of protein digestion which are formed in the intestinal lumen and are absorbed from the mucosa. These two families differ in absorption. The differences become manifest when the absorption of peptide mixtures is compared with that of equimolecular mixtures of free amino acids. The absorption of peptides occurs in two different ways: 1. Transport of intact peptides through the membrane into the mucosal cell and subsequent hydrolysis by intracellular peptide hydrolases. 2. Hydrolysis of the peptides by peptide hydrolases localized on the luminal side of the mucosal cell membrane and subsequent transport of the amino acids thus formed through the membrane. The two mechanisms of absorption do not exclude each other. The way by which energy is supplied for the transport is not yet elucidated. The transport of intact peptides is of nutritive importance only in case of dipeptides and tripeptides. It enables in particular the introduction of peptides that cannot be cleft by membrane-bound peptide hydrolases. The hydrolysis of peptides by membrane-bound peptide hydrolases and the subsequent transport of released amino acids is of importance for long-chain peptides. The difference in absorbing behaviour between the free amino acids released in the intestinal lumen and the amino acids released by peptide hydrolases at the mucosal membrane is discussed.

Amino Acids↗
PubMed1996

Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90.

To test whether an observed age-related increase in the level of oxidized protein in rat liver is due to a decrease in the activity of the multicatalytic proteinase (MCP), this protease was isolated from liver of young (8-month-old) and old (24-month-old) male Fischer 344 rats. Three peptidase activities of the MCP were assayed using fluorogenic peptides: trypsin-like, chymotrypsin-like, and peptidylglutamyl-peptide hydrolase. Only peptidylglutamyl-peptide hydrolase activity declined with age, with protease from old animals exhibiting approximately 50% of the activity of that from young animals. Bidimensional gel electrophoresis and thermostability studies did not reveal age-related structural modifications of the MCP subunits. Peptidylglutamyl-peptide hydrolase activity and trypsin-like activity were sensitive to metal-catalyzed oxidation. In some preparations, a 95-kDa protein that has been identified as the heat shock protein 90 copurified with the MCP. In the presence of HSP 90, trypsin-like activity is protected from oxidative inactivation and chymotrypsin-like activity is slightly activated. Peptidylglutamyl-peptide hydrolase activity remained sensitive to oxidation in protease isolated from young rats, but that from old rats was resistant to oxidative inactivation. Furthermore, addition of rat HSP 90 to rat liver MCP (purified from 8-month-old animals and free of contaminating HSP 90) was found to protect trypsin-like activity from oxidative inactivation.

Aging↗
PubMed1997

Proteasome inactivation upon aging and on oxidation-effect of HSP 90.

Increases of oxidatively modified protein in the cell have been associated with the aging process. Such an accumulation of damaged protein may be the result of increase in the rate of protein oxidation and/or decrease in the rate of degradation of oxidized protein. The multicatalytic proteinase or proteasome is known to be the major proteolytic system involved in the removal of oxidized protein. We have reported that, after isolation of the 20S proteasome from the liver of young and old male Fischer 344 rat, out of the three peptidase activities (chymotrypsin-like, trypsin-like and peptidyl-glutamyl peptide hydrolase) we assayed with fluorogenic peptides, the peptidyl-glutamyl peptide hydrolase activity was declining with age to a value approximately 50% of that observed for protease purified from young rats. The proteasome was subjected to metal catalyzed oxidation to determine the susceptibility of the different peptidase activities to oxidative inactivation. Both trypsin-like and peptidyl-glutamyl peptide hydrolase activities were found sensitive to oxidation. Treatment of the proteasome with 4-hydroxy-2-nonenal, a major lipid peroxidation product, was also found to inactivate the trypsin-like activity. However, the trypsin-like activity was protected from inactivation by metal catalyzed oxidation in proteasome preparations contaminated with HSP 90, a protein that often copurifies with the proteasome. Upon addition of HSP 90 to pure 20S active proteasome, the trypsin-like activity was protected from inactivation by metal catalyzed oxidation and from inactivation by treatment with 4-hydroxy-2-nonenal. These results suggest a possible intervention of HSP 90 in response to oxidative stress in preventing the inactivation of the proteasome by oxidative damage.

Aging↗
PubMed1976

Hydrolysis of peptides within lumen of small intestine.

The quantitative significance of intraluminal peptide hydrolases in the terminal stages of peptide digestion has been investigated, and the precise origins of these enzymes have been determined. Intestinal contents and mucosae were obtained from rats anethetized with ether. Experiments carried out on pancreaticobiliary secretions and germfree rats show that pancreatic and bacterial enzymes do not contribute significantly toward the luminal digestion of dipeptides. Chemical assay data, thermostability studies, and examination of electrophoretic mobilities of luminal peptide hydrolases indicate that jejunal enzymes originate predominantly from the cytoplasm of intestinal mucosal cells, whereas the brush border of muosal cells is a major source of the enzymes in the ileum. With glycl-L-phenylalanine and L-phenylalanyl-glycine as substrates, jejunal luminal activity was less than 2.6% of mucosal activity. Brush-border peptide hydrolase activity in ileal contents, however, was 11.9% and 40.7% of mucosal brush-border activity for the two substrates. Luminal enzymes thus play an insignifcant role in the terminal digestion of peptides in the jejunum, but have a much more important role in the ileal digestion of peptides.

Animals↗
PubMed1988

Rationalization of aminopeptidase activities in human skeletal muscle soluble extract.

Although a wide range of aminoacyl-7-amino-4-methylcoumarin derivatives (which are used to measure aminopeptidase activity) were found to be hydrolysed by human skeletal muscle soluble fraction, fractionation of the latter via anion-exchange and gel-filtration chromatography resolved only five types of separable aminopeptidase (with activity relative to alanyl aminopeptidase in parentheses): alanyl aminopeptidase (alpha-aminoacyl-peptide hydrolase, EC 3.4.11.14, 100%), arginyl aminopeptidase (two isoenzymes, L-arginyl-L-lysyl)-peptide hydrolase, EC 3.4.11.6, 15%); pyroglutamyl aminopeptidase (5-oxoprolyl-peptide hydrolase, EC 3.4.19.3, 3%); leucyl aminopeptidase (alpha-aminoacyl-peptide hydrolase (cytosol), EC 3.4.11.1, 1.5%) and alpha-glutamyl aminopeptidase (0.2%). Thus over 80% of the total aminopeptidase activity (expressed in relative terms) in human skeletal muscle soluble fraction can be accounted for by a single enzyme, the major aminopeptidase. A single peak of activity, which co-eluted with the major aminopeptidase after anion-exchange and gel-filtration chromatography, was obtained after assay with the following aminoacyl-7-amino-4-methylcoumarin derivatives: glycyl-, isoleucyl-, lysyl-, methionyl-, ornithyl-, phenylalanyl-, prolyl-, seryl-, tyrosyl- and valyl-. Thus, the hydrolysis of these derivatives by skeletal muscle soluble fraction occurs principally via the major aminopeptidase and not by specific enzymes, as previously suggested (Wada and Aoyagi, 1983). These results illustrate the difficulty in measuring individual aminopeptidase activities in muscle homogenate and soluble fraction, and the danger in ascribing apparent aminopeptidase activity to 'specific' enzymes.

Aminopeptidases↗
PubMed1982

Non-pancreatic hydrolysis of N-benzoyl-l-tyrosyl-p-aminobenzoic acid (PABA-peptide) in the human small intestine.

1. Hydrolysis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid (PABA-peptide) has been measured in soluble and particulate fractions of human small intestinal mucosa. 2. Both soluble and particulate fractions contained enzymic activity capable of splitting the PABA-peptide. In the particulate fractions this activity increased threefold towards the distal small intestine. 3. Neither soluble nor particulate activity was inhibited by the chymotrypsin inhibitor 1-chloro-4-phenyl-3-L-toluene-p-sulphonamidobutan-2-one (TPCK). 4. Column chromatography on Sephacryl S-300 resolved a peak of PABA-peptide hydrolase activity that was clearly distinct from other known brush-border peptide hydrolases and from added chymotrypsin standard. 5. This PABA-peptide hydrolase thus represents a distinct intestinal enzyme, possibly bound to the brush-border membrane, which could account for the residual urinary PABA recovery observed in patients and animal models with exocrine pancreatic insufficiency.

4-Aminobenzoic Acid↗
PubMed2003

Short-term CR decreases cardiac mitochondrial oxidant production but increases carbonyl content.

Lifelong caloric restriction (CR) reduces the rate of mitochondrial oxidant production and the accumulation of oxidized proteins and prevents some of the age-associated decline in 20S proteasome activity. However, few studies have investigated how rapidly the beneficial effects of CR take place. We investigated whether 2 mo of CR in 6-mo-old rats would be of sufficient duration to elicit these beneficial changes. Mitochondrial oxidant production was significantly diminished in the CR rats compared with the ad libitum-fed animals. Short-term CR also caused a significant decrease in mitochondrial superoxide dismutase (SOD) and glutathione peroxidase (GPX) activities, but there were no differences in cytosolic SOD and GPX activities, whereas mitochondrial and cytosolic catalase (CAT) activity was increased with CR. However, protein carbonyl content was significantly elevated in both the mitochondrial and cytosolic fractions from CR rats. Of the three major 20S proteasome activities (chymotrypsin-like, trypsin-like, and peptidylglutamyl-peptide hydrolase), the peptidylglutamyl-peptide hydrolase activity was significantly elevated in the CR animals, possibly because of the fact that there were more oxidized proteins to be degraded. Although fewer oxidants were produced in the CR animals, it is possible that the ability to scavenge oxidants was transiently suppressed because of the reduction in mitochondrial antioxidant enzyme activities, which may explain the observed increases in carbonyl content.

Animals↗
PubMed1979

Zymogram studies of human intestinal brush border and cytoplasmic peptidases.

Zymogram studies of peptide hydrolases from the human intestinal brush border and cytoplasmic fractions produced multiple bands--that is, up to seven--while the brush border membrane produced only a single band of enzyme activity. With all of the substrates tested except L-leucyl-L-leucyl-L-leucine, a band having anodic mobility identical with that produced by the brush border enzymes was produced by the cytoplasmic enzymes. With L-trileucine as a substrate, no overlapping band was produced. This band in the cytoplasmic fraction was heat sensitive, while that in the brush border fraction was not. Thus it would appear that there is a single human intestinal brush border peptide hydrolase capable of hydrolysing a variety of di- and tri-peptides. This peptide hydrolases of the brush border and the cytoplasmic fraction of human intestine are distinct.

Cell Membrane↗
PubMed1983

[Iron-containing proteins and the proteolytic activity in the blood serum in hyperbaric oxygenation and the protective action of urea].

The number and composition of ferro-containing proteins, the total number of iron, summary peroxidase activity and peptide-hydrolase activity have been determined under different hyperbaro-oxygenation (HBO) in blood serum. It has been established that under HBO the concentration of ferro-containing proteins increases, the fraction composition of serum and erythrocyte haemoglobin changes, the activity of acid peptide-hydrolases increases and the protamine-splitting peptide-hydrolase activity lowers. The administration of urea before HBO-experiments leads to the normalization of the most biochemical indicators of blood serum. The tests of oxygen intoxication depth assessment have been suggested.

Animals↗
PubMedDate not supplied

[Dynamics of formation of individual enzymes of the proteolytic complex during cultivation of Streptomyces griseus].

The activity of the following peptide hydrolases was studied in the course of submerged cultivation of Streptomyces griseus: proteinases (decomposing casein, benzoyl-arginine-ethyl ester, benzoyl-arginine-p-nitroanilide), carboxypeptidases, aminopeptidases, aminotripeptidases and dipeptidases (decomposing carbobenzoxy-glycyl-leucine, leucyl-glycyl-glycine, triglycine, glycyl-leucine, and glycyl-glycine). The dynamics of production differs among individual enzymes of the complex of peptide hydrolases, suggesting that they are not synthesized at the same time. The ratio between proteases in the cultural broth varies in the course of growth; therefore, the preparations with different types of action prevailing (proteinase, peptidase, etc.) can be obtained. Comparatively small changes in the composition of the medium caused considerable modifications in the processes of synthesis of peptide hydrolase and in their quantities. The overall proteolytic activity increased by a factor of 1.6 to 2.5 when the fermentation was prolonged from 120 hours to 160 to 180 hours. The most pronounced was an increase in the activity of proteinases and aminopeptidase decomposing leucyl-glycyl-glycine. These enzymes seem to be the most important in the action of the protease complex of Str. griseus.

Aminopeptidases↗
PubMed1978

[Proteolytic processes in rat brain and liver during adaptation to cold].

The autolysis and the neutral proteinase activity with respect to protamine in the brain and liver of rats were studied during cold adaptation, on the 1st, 3rd, 7th, 15th, and 45th days in the cold chamber at 2--4 degrees C. A short cold effect (1--3 days) decreases the brain autolysis by 33%, the liver one by 18%. The activity of protamine-lytic peptide-hydrolase diminishes nearly by half both in the brain and in the liver. In cold-adapted rats (45 days) the autolysis increases by 50% in the brain and by 24% in the liver. The activity of neutral peptide-hydrolase remains lowered by 43% in the brain and by 36% in the liver. Thus, only autolytic processes are intensified in cold-adapted animals while the neutral peptide-hydrolase does not participate in the increasing protein catabolism in the brain and liver.

Acclimatization↗
PubMed1985

Purification and characterization of two aminopeptidases from guinea-pig small-intestinal mucosa. Cavian intestinal tripeptide hydrolases.

Two electrophoretically distinct cytosolic peptide hydrolases from guinea-pig small-intestinal mucosa have been highly purified by a six-step procedure comprising extraction from mucosal homogenate, ammonium sulphate fractionation, DEAE-cellulose chromatography, chromatofocusing, calcium phosphate chromatography and Sephadex G-100 gel filtration. They have similar apparent molecular masses as determined by gel filtration (Mr = 68 000) or by sodium dodecyl sulphate gel electrophoresis (Mr = 72 000). Both are aminopeptidases with optimum activity at pH 7.6. They are strongly inhibited by p-hydroxymercuribenzoate, o-phenanthroline and bestatin. Although both hydrolyse some dipeptides they have a distinctive kinetic preference for tripeptides composed of aromatic or non-polar residues. Their affinities for some tripeptides are particularly high and also the hydrolysis of some substrates exhibits biphasic kinetics. These two aminotripeptidases are similar but they can be differentiated from each other and from a number of other aminopeptidases.

Aminopeptidases↗