Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.25.1 (proteasome)
 28,817 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two trials were conducted to determine the influence of realimentation diet energy, protein, B-vitamin (BV) and Lactobacillus acidophilus (LAC) content on recovery of rumen activity and feed consumption in beef steers. In trial 1, ruminal-fistulated steers were fasted and refed 1) prairie hay, 2) 10% protein (LCP), 3) 12.5% protein (MCP), 4) LCP + BV or 5) LCP + LAC. In trial 2, calves were fasted and refed 1) 60% cottonseed hulls-40% alfalfa dehy (high roughage), 2) LCP, 3) 15% protein (HCP), 4) LCP + BV or 5) LCP + LAC. Rumen fermentative capacity declined 74% (P less than .05) during feed and water deprivation, but returned to control levels by d 7 of realimentation. On d 3 of realimentation, steers fed the LCP and MCP diets had molar proportions of ruminal butyrate in excess of 35%. Steers fed the hay, LAC and BV diets did not have a high butyrate fermentation. In trial 2, calves lost about 15% of their body weight during feed and water deprivation. Calves fed the high roughage diet appeared to return to prefast feed and energy intakes more slowly than steers fed the medium roughage diets. Results of this study indicate that rumen fermentative capacity is a factor limiting feed intake in fasted calves for 7 to 14 after the reintroduction of feed and water.
J Anim Sci 1985 Sep
PMID:Influence of realimentation diet on recovery of rumen activity and feed intake in beef steers. 299 54

Some regularities of the enzyme immunoassay (EIA) of whole bacterial cells have been studied on one of the bacillary species of contaminant microflora. Early detection of this microorganism is highly important for the microbiological production of alpha-amylase and alkaline protease (produced by Bacillus subtilis). The effective kinetic and equilibrant parameters of the interaction of peroxidase-labeled antibodies with the cells of the contaminant microflora in the solution and on the surface of the polystyrene plates have been defined. Two methods for the separation of cells after their interaction with peroxidase-labeled antibodies have been optimized: filtration involving the use of special filter plates and centrifugation in plates. The method for the immobilization of cells in the wells of standard assay plates by centrifugation has been proposed. Four EIA methods for measurement of contaminant microflora have been developed and optimized. These methods permit the determination of the microflora at concentration of 5 X 10(5)-5 X 10(4) cells/ml, depending on the scheme of the assay, within 1-3.5 minutes.
Zh Mikrobiol Epidemiol Immunobiol 1987 Sep
PMID:[Patterns in the immunoenzyme analysis of bacterial cells]. 312 Apr 44

Two pathogenic mechanisms of Pseudomonas aeruginosa corneal infections are discussed, one involving bacterial exoenzymes, the other involving polymorphonuclear leukocyte (PMN)-derived lysosomal enzymes. The objective of the present study was (1) to show the relative importance of the two mechanisms and (2) to evaluate the effect of active immunization against P. aeruginosa exoenzymes on ocular damage. Rabbits were immunized against P. aeruginosa alkaline protease (AP) or elastase (Ela) and challenged with the respective enzymes. Corneal damage was studied by light photography (LP). In another group, rabbits were immunized against AP, Ela and exotoxin A (ExoA) and challenged with P. aeruginosa strains PA01 or PA103. Corneal damage was studied with LP, light microscopy, and electron microscopy. Immunized animals were totally protected against intracorneal inoculation of P. aeruginosa proteases. Twelve hr and 24 hr after challenge with whole bacteria, immunized rabbits revealed less corneal damage than non-immunized animals. However, after 48 hr corneal damage (ie severe corneal ulceration) was comparable in both groups. The study suggests that corneal damage involving lysosomal enzymes from stimulated PMN is more important after bacterial infection than direct damage by P. aeruginosa exoenzymes.
Invest Ophthalmol Vis Sci 1987 Sep
PMID:Relevance of host-derived and bacterial factors in Pseudomonas aeruginosa corneal infections. 330 11

An alkaline proteinase, previously identified in rat liver and heart, has been purified from the soluble fraction of human erythrocytes. The proteinase has an apparent molecular weight of 600 000 and is composed of eight subunits with molecular weights ranging from 32 000 to 21 000. The proteinase degrades both protein and synthetic peptide substrates with a broad pH optimum of 7.5-11.0. Among the synthetic peptides tested, tripeptides with arginine at the P1 position (e.g. Z-Val-Leu-Arg-4-methoxy-2-napthylamine and Boc-Leu-Gly-Arg-4-methylcoumarin-7-amide) are particularly good substrates. The proteinase appears to be sulfhydryl-dependent and is inhibited completely by mersalyl acid and by hemin; inhibitors of serine and metallo-type proteinases have no effect on proteinase activity. Interestingly, a variety of other proteinase inhibitors such as leupeptin, chymostatin and N-ethylmaleimide failed to completely inhibit protein-hydrolyzing activities of the enzyme. These results indicate that these activities may be accounted for by at least two different catalytic sites. Proteinase activity is stable in the presence of 1 M urea, 0.5% Triton X-100 or 0.03% SDS and is not affected by ATP. Based on the high molecular weight and sulfhydryl-dependence, we have named this proteinase macropain.
Biochim Biophys Acta 1986 Sep 26
PMID:Purification and characterization of a high molecular weight proteinase (macropain) from human erythrocytes. 353 Mar 30

A high-molecular-mass protease, ingensin, was purified to homogeneity from rabbit reticulocytes by DEAE-cellulose, HPLC gel filtration, and hydroxyapatite chromatographies. By these procedures, ingensin activity was separated from the activities of two other unique aminopeptidases, one of which is activated by ATP. Ingensin had the following properties: the optimum activity was seen around pH 9.0 and at 50 degrees C; addition of 0.04% SDS and 1 mg/ml linoleic acid resulted in 8- and 4-fold increases in peptide-hydrolyzing activity, respectively. The molecular mass was found to be 700,000 +/- 100,000 daltons on gel filtration, but SDS electrophoresis revealed that the enzyme is composed of several subunits with molecular weights of less than 35,000. The N-terminal-blocked tyrosine- and arginine-MCA derivatives, but not Arg-MCA, were hydrolyzed rapidly by ingensin. The approximate Km values for the reaction of ingensin with Suc-Leu-Leu-Val-Tyr-MCA and Z-Ala-Arg-Arg-MCA were 0.32 and 0.12 mM, respectively. The degradation of several proteins in the reticulocyte extract was stimulated by the addition of SDS and linoleic acid. The activator concentrations necessary for stimulation of the protein hydrolysis are similar to those of the purified reticulocyte ingensin for synthetic substrates. Ingensin did not associate with either right-side-out or inside-out red cell membranes. These results suggest that ingensin is a cytosolic fatty acid-stimulated protease, which is involved in the protein turnover in reticulocyte extracts.
J Biochem 1986 Sep
PMID:Ingensin, a high-molecular-mass alkaline protease from rabbit reticulocyte. 353 97

Two forms of a neutral protease that catalyzed the hydrolysis of succinyl-Leu-Leu-Val-Tyr-MCA were isolated from porcine skeletal muscle cytosol by fractionation on DEAE-cellulose, hydroxyapatite and Sephadex G-100. The native enzyme had a molecular mass of above 1000 kDa. Peak A, which was eluted from hydroxyapatite at 50 mM phosphate, was activated 37-fold by the detergent, SDS, while peak B which was eluted at 150 mM phosphate, was activated only 2-fold. After dialysis against water, the B form showed restored ability to be activated by SDS (9.6-fold with 0.04% SDS). The activated peak B was extremely sensitive to divalent and monovalent cations such as Ca2+, Mg2+, Na+, K+ and NH+4 as well as protease inhibitors such as leupeptin, chymostatin and DFP. These results suggest that these proteases are generally latent in the cells and may be regulated by changes in the concentrations of cations in the cytosol. We call this new type of protease, ingensin.
FEBS Lett 1985 Sep 09
PMID:Isolation of two forms of the high-molecular-mass serine protease, ingensin, from porcine skeletal muscle. 389 52

We investigated the role of Pseudomonas aeruginosa exoenzymes in cystic fibrosis lung infection in the presence and absence of specific serum antibodies. In sputa of 21 cystic fibrosis patients, concentrations of P. aeruginosa proteases and exotoxin A were determined by sensitive radioimmunoassays. In all sputa, detection of exoenzymes was negative (less than or equal to 10 ng). Positive serum antibody titers to bacterial exoenzymes were found in the majority of patients. Purified immunoglobulin G (IgG) preparations from the sera of two patients revealing specific antibody titers to the bacterial proteases neutralized these enzymes at ratios of 1,000:1 to 5,600:1 (wt/wt). Above the neutralizing capacity of IgG, proteases caused cleavage of IgG; below that level, no enzymatic activity was observed. In vitro incubation of P. aeruginosa elastase, alkaline protease, or exotoxin A with elastase derived from polymorphonuclear leukocytes showed that polymorphonuclear leukocyte elastase: (i) was cleaved by bacterial elastase, (ii) was not inactivated by alkaline protease, and (iii) inactivated exotoxin A. The results suggest that soon after the onset of P. aeruginosa lung infection in cystic fibrosis patients, bacterial proteases, but not exotoxin A, become important virulence factors. The results also suggest that exoenzymes do not directly contribute to lung damage after immune response to bacterial antigens has begun.
Infect Immun 1985 Sep
PMID:Role of Pseudomonas aeruginosa exoenzymes in lung infections of patients with cystic fibrosis. 392 91

An intensive parasexual genetics program in which industrial strains of Penicillium chrysogenum were used culminated in the isolation of a number of heterozygous diploid strains. The diploid clones were selected from heterokaryons formed from matings between mutant strains having complementary biochemical and conidial color markers. Several diploid cultures were compared with their haploid wild-type parents and other distantly related production strains on the basis of a variety of cultural and physiological criteria. The diploid strains characteristically produced conidia of larger volume and higher deoxyribonucleic acid content. Some were vigorous with respect to growth rate and onset and degree of conidiation. One diploid strain (WC-9) had a 46% greater oxygen uptake rate and oxidized glucose at a 57% greater rate than its haploid parent (M-2). It also produced 33% higher concentrations of beta-galactosidase, 66% more alkaline protease, and 53% more glucose oxidase than the M-2 haploid parent. The selection of rare stable diploid mold cultures through the use of parasexual genetics offers a unique approach to the direct selection of mutants with potential for increased enzyme formation.
Appl Microbiol 1971 Sep
PMID:Biochemical properties of haploid and diploid strains of Penicillium chrysogenum. 511 5

The genes for alkaline protease (apr[BamP]) and neutral protease (npr[BamP]) from Bacillus amyloliquefaciens have been isolated and expressed in Bacillus subtilis. The DNA sequences of apr[BamP] and npr[BamP] revealed, in each case, the presence of a large open reading frame. The inferred amino acid sequence of either gene contained a signal sequence and an additional polypeptide sequence ('pro' sequence) preceding the mature protein. Based on DNA sequence, the start point of translation has been identified as amino acid residue - 107 for apr[BamP] and -221 for npr[BamP]. To demonstrate that the start point of translation of apr[BamP] in vivo is probably at codon -107, codon -103 (AAA) was changed to an ochre (TAA) by site-directed mutagenesis. Alkaline protease was produced from this ochre mutant derivative of apr[BamP] only when the host strain was Su+. The presence of a pro sequence may be common to all of the secreted proteases from bacilli.
J Bacteriol 1984 Sep
PMID:Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein. 609 Mar 91

The production of alkaline protease, collagenase and histidine utilization (Hut) enzymes by Vibrio alginolyticus wild-type, hutH1 and hutU1 strains was investigated. Alkaline protease synthesis was stimulated by histidine and urocanic acid in the wild-type and hutU1 strains. The hutH1 mutant alkaline protease production was stimulated by urocanic acid and not by histidine. The Hut enzymes in the wild-type strain were coordinately induced by histidine. Urocanase and formimino-hydrolase were induced by histidine in the hutH1 mutant which lacked histidase and was not able to convert histidine to urocanic acid. Collagenase production in peptone medium was inhibited in the hut mutants. It is concluded that in V. alginolyticus urocanic acid regulates alkaline protease synthesis but that the Hut enzymes are induced by histidine. The involvement of the Hut genetic system in the regulation of alkaline protease and collagenase synthesis is discussed.
J Gen Microbiol 1982 Sep
PMID:Regulation of hut enzymes and intracellular protease activities in Vibrio alginolyticus hut mutants. 612 84


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