THE ACTIVATION OF ALPHA-CHYMOTRYPSINOGEN WITH PROTEINASE OF STREPTOMYCES GRISEUS.
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Chromatography↗
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Results for “PEPTIDE HYDROLASES”
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[POLAROGRAPHIC CONTROL OF FIBRINOGEN DEGRADATION BY THE PROTEOLYTIC ENZYME ("PRONASE") OF STREPTOMYCES GRISEUS].
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Animals↗
[Proteinase activity in the early developmental stages of the carp, Cyprinus carpio].
Embryonic and early postembryonic development of the carp is associated with an increase in the content of soluble proteins and nitrogen of non-protein nitrogenous components. Simultaneously, the activity of trypsin-like and chemotrypsin-like peptide hydrolases increases together with the increase in the degree of proteolysis. These data suggest that the development of carp embryos and early larva is accompanied by intensification of two opposite processes--synthesis and catabolism of proteins. The observed changes are more evident in early postembryonic period as compared with the early stages of embryogenesis.
Animals↗
[SOME PROPERTIES OF HIGHLY PURIFIED PROTEASE FROM CL. BOTULINUM B].
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Botulinum Toxins↗
Nonpancreatic hydrolysis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid (PABA peptide) in the rat small intestine.
Factors affecting the intestinal hydrolysis of orally administered N-benzoyl-L-tyrosyl-p-aminobenzoic acid (PABA peptide) and urinary recovery of p-aminobenzoic acid have been studied in rats, after diversion of the pancreatic and biliary secretions. The exclusion of pancreatic secretions from the small intestine lowered, but did not completely abolish, the urinary recovery of PABA, whereas diversion of the bile had no significant effect. A particulate-bound enzyme capable of splitting PABA peptide was found to be present throughout the rat small intestine, and its activity remained unchanged in the absence of biliopancreatic secretions. The intestinal PABA peptide hydrolase could be solubilized with papain and Triton from a partially purified brush-border membrane fraction, and it eluted in gel filtration as a high-molecular-weight peak, well separated from the other known peptidases of the intestinal brush-border membrane.
4-Aminobenzoic Acid↗
USE OF A PROTEASE OF STREPTOMYCES GRISEUS IN TISSUE CULTURE.
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Endopeptidases↗
[Effect of EGF on the activity of nuclear and cytoplasmic 26S proteasomes in A431 cells].
It has been first shown that EGF regulates a proteolytic activity of proteasomes. Following a 15 min action with 100 ng/ml EGF, three types of peptidase activity of both cytoplasmic and nuclear proteasomes were induced in A431 cells, although, this effect on different populations of proteasomes was selective. EGF preferentially stimulates chymotrypsin-like activity of cytoplasmic proteasomes, and induces a similar increase of chymotrypsin-like, trypsin-like and peptydylglutamyl peptide hydrolase activities of nuclear particles. Tyrphostin, an inhibitor of tyrosine kinase activity of EGF receptor, prevents the EGF effect on both proteolytic and RNase activity of nuclear and cytoplasmic proteasomes. It is concluded that EGF may rapidly and selectively stimulate enzymatic activity of EGF receptor.
Cell Line, Tumor↗
[Immobilized form of Streptomyces griseus proteases complex].
The immobilized form of proteases complex of Str. griseus actinomycete is obtained by means of glutaric aldehyde with aminoethyl cellulose. Hydrolysis of synthetic substrates showed that the system of peptide hydrolases is bound, but the ratio of activities as compared to the initial proteolytic complex changes, pH-optimum of the total proteolytic activity, pH- and temperature optima of stability are not changed with immobilization. On the whole no essential stabilization of the complex was observed. After five repeated cycles of the immobilized form utilization of the activity loss accounts for 40-60%.
Enzymes, Immobilized↗
Structural and functional characterization of 20S and 26S proteasomes from bovine brain.
Two proteins were isolated, in a stable form, from bovine brain by ion exchange chromatography, gel filtration and ultracentrifugation on glycerol gradient. They were identified as 20S and 26S proteasomes on the basis of molecular mass, migration velocity on non-denaturing gels, immunoreactivity, multipeptidase activity and the 26S proteasome also for dependence on ATP for the degradation of short peptides and ubiquitinylated proteins. However, the 26S proteasome has some properties not yet described for its counterpart of other tissues and from brain of this and other species. In particular, the ATP concentration required by the 26S proteasome to reach maximal peptidase activity was approximately 40-fold lower than the one required for maximal proteolytic activity on polyubiquitinylated substrates. Moreover, plots of substrate concentration vs. velocity gave a saturation curve for the 26S proteasome only, which, for the trypsin-like and post-glutamyl peptide hydrolase activities fitted the Michaelis-Menten equation, whereas for the chymotrypsin-like activity indicated multibinding site kinetics with positive cooperativity (n = 2.32+/-0.38). As concerns the 20S proteasome, its electrophoretic pattern on native gel revealed a single protein band, a feature, to our knowledge, not yet described for the brain particle of any species.
Animals↗
The effect of alpha-ketoglutaric acid on amino acid utilization by nonstarter Lactobacillus spp. isolated from Cheddar cheese.
AIMS: To examine the effect of alpha-ketoglutaric acid (alpha-KG) on the utilization and catabolism of amino acids by strains of nonstarter lactobacilli isolated from Cheddar cheese. METHODS AND RESULTS: The effect of alpha-KG in the growth medium of nonstarter lactobacilli on amino acid metabolism, catabolite levels, peptide hydrolase and aminotransferase activities was examined. The pattern of amino acid utilization, catabolite formation and aminotransferase activity was affected by keto acid. CONCLUSIONS: Amino acid conversion into cheese aroma and flavour compounds by nonstarter lactobacilli is enhanced in the presence of alpha-ketoglutarate. SIGNIFICANCE AND IMPACT OF THE STUDY: Increasing the availability of alpha-ketoglutarate in cheese offers a possible method of reducing the maturation period by accelerating the rate of character compound formation from amino acids by the nonstarter lactobacilli.
Amino Acids↗
Nine polymorphic markers characterized by polymerase chain reaction techniques form two linkage groups on rat chromosome 8.
Five genes and four anonymous polymorphic markers, forming two linkage groups, were mapped in F2 intercross progeny of F344/N x LEW/N rats using polymerase chain reaction (PCR) techniques. Both linkage groups were assigned to rat chromosome 8 because they contained genetic loci previously mapped to this chromosome. The first group was comprised of markers for three anonymous loci and two gene loci, thymus cell antigen-1 (Thy1) and tropoelastin (Eln). The second group was comprised of markers for one anonymous locus and three gene loci, cellular retinol binding protein II (Rbp2), matrin F/G (Matr1), and acyl-peptide hydrolase (Apeh). Seven markers (identified by simple sequence repeat associated length polymorphisms) were characterized in an additional 13 inbred rat strains (ACI/N, BN/SsN, BUF/N, LER/N, LOU/MN, MNR/N, MR/N, SHR/N, SR/Jr, SS/Jr, WBB1/N, WBB2/N, and WKY/N). Two to six alleles were detected for each marker. The reported markers should facilitate genetic mapping and monitoring of inbred rat strains.
Alleles↗
Thyrotropin-releasing hormone-like material in the rat retina: changes due to environmental lighting.
Material reacting with an antibody to thyrotropin-releasing hormone (TRH) has been found to be present in the rat retina. The compound present in the retina cochromatographed with authentic TRH and most of its activity was lost when incubated with pyroglutamate aminopeptidase (L-pyroglutamyl-peptide hydrolase, EC 3.4.11.8), an enzyme that degrades TRH. The TRH-like activity in the rat retina was low during the night and high during the day. There was a 4-hr lag period after the lights were turned on before peak TRH levels were attained. A decrease in TRH was seen after 2 hr of darkness and the level of TRH was lowest after 4 hr of darkness. Retinal TRH is elevated by environmental lighting regardless of the time of the day. These findings suggest that TRH may be involved in retinal photorecptive mechanisms.
Animals↗
Muscular dystrophy and activation of proteinases.
Evidence is presented for the existence of many different systems of proteolytic enzymes in human skeletal muscle. These include the lysosomal system of cathepsins as well as proteinases and peptide hydrolases that are optimally active at neutral and alkaline pH ranges. The majority of proteolytic enzymes examined are found to show increased activity in dystrophic human muscle. Moreover, a high initial rise is observed in cathepsin B1, a thiol-dependent endopeptidase of lysosomes, and in dipeptidyl peptidase IV, a membrane-associated peptidase. In addition, a calcium-activated neutral proteinase is found to be significantly elevated in muscle from patients with Duchenne dystrophy. The possible roles of these proteinases in intracellular protein catabolism and muscle wasting are discussed.
Aminopeptidases↗
Influence of retention time on degradation of pancreatic enzymes by human colonic bacteria grown in a 3-stage continuous culture system.
Hydrolytic enzymes were measured in gut contents from four sudden death victims. Pancreatic amylase and total protease activities decreased distally from the small bowel to the sigmoid/rectum region of the large intestine, showing that considerable breakdown or inactivation of the enzymes occurred during gut transit. To determine whether pancreatic enzymes were substrates for the gut microflora, mixed populations of bacteria were grown in a 3-stage continuous culture system on a medium that contained pancreatic extract as the sole nitrogen source. The multichamber system (MCS) was designed to reproduce in vitro, the low pH, high nutrient, fast growth conditions of the caecum and right colon and the neutral pH, low nutrient, slow growth conditions of the left colon. Results showed that pancreatic amylase was resistant to breakdown by intestinal bacteria compared with the peptide hydrolases in pancreatic secretions. Leucine aminopeptidase, trypsin and to a lesser degree, chymotrypsin, were easily degraded by gut bacteria, but pancreatic elastase was comparatively resistant to breakdown. Protein degradation in the MCS, as determined by enzyme activities, protein concentration and ammonia and phenol production, increased concomitantly with system retention time over the range 24-69 h. These results suggest that intestinal bacteria play an important role in the breakdown of hydrolytic enzymes secreted by the pancreas and that this process and protein fermentation in general, is likely to occur maximally in individuals with extended colonic retention times.
Amylases↗
[Effect of arginine on the activity of proteolytic enzymes in the rat brain and liver].
The influence of arginine on autolysis and proteolysis was studied. Arginine at the concentration of 0.5 and 1.0 microM/ml was added to the incubation mixture. Proteolytic processes were studied in the acid, neutral and alkaline media (pH 4.5; 7.4; 8.5). Autolysis was determined by incubation of the brain and liver homogenates and proteolysis by the use of bovine serum albumin as a substrate. Autolytic and proteolytic activities were calculated as an increase of Folin positive compounds or amino nitrogen in the samples. It was established that the influence in vitro of arginine on the proteolytic processes depended on pH, type of the peptide-hydrolases, to a lesser extent, on the arginine concentration and did not depend on the tissue type. Arginine displayed its regulative action in the brain and liver by the same way. The addition of arginine had an effect on autolysis and proteolysis in the neutral and alkaline media. Determination of autolytic and proteolytic activities by Folin positive compounds has shown that arginine addition into the samples decreased autolysis and proteolysis. At the same time determination of autolysis and proteolysis by amino nitrogen in the presence of arginine has shown that autolytic and proteolytic activities increased.
Animals↗
[Hydrolase from Xanthomonas rubrilineans for synthesis of cefalexin].
The use of peptide hydrolase (EC 3.4.13.1) from Xanthomonas rubrilineans for synthesis of the antibiotic cephalexin from 7-aminodesacetoxycephalosporanic acid was studied. The optimum conditions for production of cephalexin were determined, and the yield exceeded 80%. A method for monitoring the synthesis of this antibiotic synthesis by means of a conventional amino acid analyzer is proposed.
Cephalexin↗
Peptidase activities of the 20/26S proteasome and a novel protease in human brain.
Many neurodegenerative diseases are characterized by ubiquitin-positive protein aggregates or inclusion bodies. Ubiquitin-conjugated proteins are degraded by the 20/26S proteasome, and reduced proteasome peptidase activities in brain homogenates have been reported in pathologic lesions of Parkinson's and Alzheimer's diseases. However, it is unknown whether crude extracts of human brain contain other proteases having peptidase activities. We found a novel protease of molecular weight of approximately 105 kDa in normal human brain, which exhibited trypsin-like (T-L) and chymotrypsin-like (ChT-L) activities (corresponding to 52% and 21% of the total activities in crude extracts) but not peptidyl glutamyl peptide hydrolase activity. Both T-L and ChT-L activities of this protease were partially inhibited by proteasome inhibitors (MG132, lactacystin) and, in contrast to those of the proteasome, also by sodium dodecyl sulfate. A simple method to obtain a brain fraction specific to the 20/26S proteasome was developed. Our human brain data suggest that T-L and ChT-L activity levels of the proteasome reported previously may include those of the 105 kDa protease, an enzyme of as yet unknown biological significance, and that it is necessary to separate the proteasome from this protease to evaluate the actual status of the ubiquitin-proteasome system in neurodegenerative disorders.
Aged↗
Different pathways for lysine transport across neonatal pig intestine.
1. Undirectional fluxes of lysine, presented free and in the form of a dipeptide, have been measured in vitro using the small intestines of pigs taken during the first 2 weeks of post-natal life. 2. The concentration dependence of free lysine transfer to the serosal surface of new-born pig intestine (Jms) can be described as the sum of a saturable (Km 0.2 mM; Jm 3 n- mole cm-2 in-1) and a non-saturable (1.0 n-mole cm-2 min-1 mM-1) component. 3. The dipeptide isoleucyl-lysine was hydrolysed completely during transfer to the serosal surface of intestines taken at all stages of development. The concentration dependence of peptide-derived lysine transfer can be described as if it took place through a single saturable process (Km 5 mM; Jm 27 n-mole cm-2 min-1). 4. The mucosa to serosa transfer of free lysine fell to a half and that of peptide-derived lysine fell to a quarter, during the first 8 days of post-natal life. The decline in peptide-derived lysine transport correlated with changes in peptide hydrolase activity, measured in homogenates of intestinal mucosa using isoleucyl-lysine as substrate. 5. The new-born pig intestine transported lysine derived from isoleucyl-lysine twice as quickly as from lysyl-isoleucine. Lysine and isoleucine did not inhibit the transfer of isoleucine and lysine derived from isoleucyl-lysine. The transport of lysine, but not isoleucine, from isoleucyl-lysine took place more quickly than from equimolar solutions of the free amino acids. 6. It is suggested from these results that lysine and isoleucyl-lysine use different pathways when crossing the intestinal mucosa. Attempts are made to assess the probable contributions made by these pathways to the total absorption of lysine taking place during neonatal development.
Animals↗