Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Urinary MDH, LDH, gamma-GT, LAP and muramidase levels were studied in 11 healthy persons with a wide age range and in 51 male Winstar rats weighing 300 to 400 g. Normal ranges of these urinary enzymes were determined and compared with the results of other authors.
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PMID:[Urinary enzyme levels in healthy human subjects and in rats (author's transl)]. 0 74

Biochemical composition of middle ear effusions (MEE) and serum was compared both in experimentally induced middle ear inflammation in squirrel monkeys and in otitis media in humans. The MEE and serum protein concentrations were similar in the animal experiments. In human MEE the total protein concentration of both serous and mucoid effusions was higher than the proteins of the serum. High concentrations of potassium and lower concentrations of glucose in human MEE than in serum were also observed. Activities of various oxidative (lactate dehydrogenase, malate dehydrogenase) and hydrolytic (leucine aminopeptidase, alkaline and acid phosphatase, and lysozyme) enzymes in MEE and serum were compared. The ratio of enzyme activity between MEE and serum (MEE/Serum) was greater than one in all enzymes studied. Mucoid MEE had higher activity of enzymes than serous effusions in general. Lactate dehydrogenase isoenzyme patterns were compared on electropherogram. Isoenzyme fractions 1 and 2 were each smaller in MEE than in serum whereas 4 and 5 had a significantly higher activity in MEE than in serum. Higher activities of enzymes in MEE as compared with serum are consistent with the hypothesis that MEE results from inflammatory processes occurring in the middle ear cavity. The enzymes of MEE seem to have multiple origins, namely, 1) enzymes normally present in blood, 2) enzymes from the inflamed middle ear mucosa, and 3) enzymes from leucocytes present in effusions.
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PMID:Biochemical characteristics of middle ear effusions. 81 35

Activities of various oxidative (LDH, MDH) and hydrolytic (LAP, alkaline- and acid phosphatase, and lysozyme) enzymes in serous middle ear effusions (MEE) and serum from patients with serous otitis media were studied. The ratio of enzyme activity between MEE and serum (MEE/serum) was greater than one for all enzymes studied indicating a higher activity of these enzymes in MEE than in serum. These findings are consistent with a hypothesis suggesting the release of enzymes from inflammatory processes in the middle ear cavity. These enzymes presumably originate from 1) enzymes normally present in blood, 2) release of enzymes from inflamed middle ear mucosa, 3) release of enzymes from inflammatory cells present in the effusions.
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PMID:Certain oxidative and hydrolytic enzymes in the middle ear effusion in serous otitis media. 98 18

The hydroxyl groups of poly(ethyleneglycol) have been esterified (partly) with a number of carboxylic acids. When these esters are included in dextranpoly(ethyleneglycol)-water biphasic systems the partitions of proteins and membranes between the two phases (and the interface) are in some cases strongly affected. The affinity of serum albumin for the poly(ethyleneglycol)-rich phase is strongly increased when the fatty acid group consists of more than 10 carbon atoms. The partition also depends on the number of double bonds in the fatty acid. A corresponding relationship is found for membranes from spinach chloroplasts. The partitions of ovalbumin, lysozyme (EC 3.2.1.17) and ribonuclease (EC 3.1.4.22) are not influenced by the fatty acid esters. Esters of dibasic carboxylic acids show a minute but marked effect on the partition of proteins in general while malate and tartrate esters affect strongly the partition of chloroplast membranes. The partitions of both proteins and membranes are influenced by poly(ethyleneglycol) deoxycholate. Experiments with malate dehydrogenase (EC 1.1.1.37), lactate dehydrogenase (EC 1.1.1.27), fumarase (EC 4.2.1.2), enolase (EC 4.2.1.11) and glutamate-ocaloacetate transaminase (EC 2.6.1.1) show that their partitions, measured on enzymic activity basis, is changed when esters of benzoic, linolenic, tartaric or deoxycholic acid are included in the biphasic system. The mechanism behind the effect of the esterified poly (ethyleneglycol) on the partition of biomaterial, in this type of aqueous biphasic systems, is discussed in terms of a direct binding of the esters to the partitioned material.
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PMID:The effect of poly(ethyleneglycol) esters on the partition of proteins and fragmented membranes in aqueous biphasic systems. 99 68

A description is given of an outbreak of equine infectious anaemia (E.I.A.) in Campania [at Naples and Aversa (Caserta)]; it was diagnosed by clinical, pathological and serological examinations (Coggins test). Using the serum of 45 horses with E.I.A. and 11 healthy horses (controls), numerous investigations were carried out on: enzymes, intrinsic coagulation factors, lipids and other substances. The results obtained were very interesting and show that in this disease there are significant increases in many enzymes (LDH, LAP, gamma-GT, CPK, PK and ALD) and copper. Insignificant increases were found in other enzymes (SDH, GLDH, MDH, ICDH, AIP, lysozyme, cholinesterase, GOT and GPT) and also intrinsic coagulation factors, lipid substances (total cholesterol, esterified cholesterol, triglycerides) and glucose. LDH-1-isoenzyme remains unchanged, whilst AcP decreases slightly.
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PMID:Biochemical studies on equine infectious anaemia. 101 May 2

The circular dichroism bands of (+) gossypol in the spectral region 300-400 nm have been shown to be sensitive to interactions with proteins. Using CD spectroscopy, gossypol has been shown to interact with lactate dehydrogenase, malate dehydrogenase, alkaline phosphatase, lysozyme, protamine and poly-L-lysine. Binding to proteins generally results in a pronounced red shift of the long wavelength CD band (approximately 380-430 nm) accompanied by a reduction in ellipticity. The changes in spectral parameters of the 1Lb binaphthyl transition may reflect a distortion from a nearly perpendicular gossypol conformation, on binding to proteins.
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PMID:A circular dichroism study of (+) gossypol binding to proteins. 674 22

Polymorphonuclear leucocytes were isolated from pig blood relatively free from other cells and were characterised biochemically and morphologically and compared with human PMNLs. The activities of 16 enzymes of porcine and human PMNLs were measured and compared. Alkaline phosphatase, acid phosphatase, phosphodiesterase, gamma-glutamyl transpeptidase, NADH-cytochrome c oxidoreductase, malate dehydrogenase and acetylcholinesterase had higher specific activities in procine than in human cells. Alkaline phosphatase has an 87-fold higher specific activity in porcine than in human cells. beta-glucuronidase, lysozyme, beta-galactosidase, N-acetyl-glucosaminidase, beta-glucosidase, myeloperoxidase and catalase had higher specific activities in human than in porcine cells. beta-glucuronidase and myeloperoxidase showed over a 1000- and a 13-fold higher specific activity, respectively, in human than in porcine cells. Porcine PMNLs are readily available in large numbers and are recommended for studies of phagocytosis, chemotaxis and membrane biochemistry.
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PMID:Biochemical characterisation of porcine polymorphonuclear leucocytes: comparison with human polymorphonuclear leucocytes. 687 22

Fumarase (EC 4.2.1.2) and mitochondrial L-malate dehydrogenase (EC 1.1.1.37) were both inhibited by NaAuCl4 and KAuBr4. The inhibition for both was measured as a function of gold complex concentration and aquation time, and the NaAuCl4 inhibition was also measured in the presence of 0.15 M NaCl. Regeneration of the enzyme activity after NaAuCl4 inhibition using L-cysteine, L-methionine and NaCN was also investigated. Sodium dodecyl sulfate (SDS) acrylamide gel electrophoresis and amino acid analysis was performed on the NaAuCl4 inhibited enzymes as well as on ribonuclease A (EC 3.1.26.2), lysozyme (EC 3.2.1.17) and liver alcohol dehydrogenase (EC 1.1.1.1). It was observed that the inhibition was proportional to the gold complex concentration but decreased markedly after aquation of the complex. In the presence of NaCl the initial rate of inactivation is essentially unaffected unless the complex has been aquated and then the initial rate is increased. Gel electrophoresis on gold complex-enzyme mixtures show polymerization for ribonuclease and lysozyme and amino acid analysis indicates that no oxidation has taken place. From these results, a binding mechanism is postulated for the inhibition of the dehydrogenases by direct displacement of a halide ligand, probably by two groups on the enzyme, at least one of which may be a sulfur containing acid.
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PMID:Inhibition of two mitochondrial enzymes by gold (III) halo complexes. Evidence for a binding mechanism. 715 Dec 34

1. A method is described for preparing spheroplasts from Paracoccus denitrificans that are substantially depleted of dissimilatory nitrate reductase (cytochrome cd) activity. Treatment of cells with lysozyme + EDTA together with a mild osmotic shock, followed by centrifugation, yielded a pellet of spheroplasts and a supernatant that contained d-type cytochrome. The spheroplasts were judged to have retained an intact plasma membrane on the basis that less than 1% of the activity of a cytoplasmic marker protein, malate dehydrogenase, was released from the spheroplasts. In addition to a low activity towards added nitrite, the suspension of spheroplasts accumulated the nitrite that was produced by respiratory chain-linked reduction of nitrate. It is concluded that nitrate reduction occurs at the periplasmic side of the plasma membrane irrespective of whether nitrite is generated by nitrate reduction or is added exogenously. 2. Further evidence for the integrity of the spheroplasts was that nitrate reduction was inhibited by O2, and that chlorate was reduced at a markedly lower rate than nitrate. These data are taken as evidence for an intact plasma membrane because it was shown that cells acquire the capability to reduce nitrate under aerobic conditions after addition of low amounts of Triton X-100 which, with the same titre, also overcame the permeability barrier to chlorate reduction by intact cells. The close relationship between the appearance of chlorate reduction and the loss of the inhibitory effect of O2 on nitrate reduction also suggests that the later feature of nitrate respiration is due to a control on the accessibility of nitrate to its reductase rather than on the flow of electrons to nitrate reductase.
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PMID:The location of dissimilatory nitrite reductase and the control of dissimilatory nitrate reductase by oxygen in Paracoccus denitrificans. 719 18

Two types of superoxide dismutase (SOD) have been found in Brucella abortus, a cytosolic Mn-SOD and a Cu/Zn-SOD of unknown location. We sought to determine the subcellular location of Cu/Zn-SOD in B. abortus ST 19. We report a modified spheroplasting procedure for the release of periplasmic contents from B. abortus cells using a dipolar ionic detergent, Zwittergent 316. This detergent, used in place of EDTA, destabilizes the outer membrane sufficiently to allow penetration of lysozyme and the subsequent selective release of periplasmic proteins by osmotic shock. Cytoplasmic cross-contamination of periplasmic fractions was assessed by assaying for malate dehydrogenase activity. Cyanide-sensitive and cyanide-insensitive SOD activity was measured by both the xanthine oxidase-cytochrome c method and a hematoxylin assay. Results suggest that B. abortus Cu/Zn-SOD activity is periplasmic. This zwittergent-lysozyme extraction procedure may be applicable to the separation, isolation and characterization of many other periplasmic proteins of B. abortus and other Gram-negative organisms especially when cytosolic contamination is undesirable.
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PMID:Periplasmic location of Brucella abortus Cu/Zn superoxide dismutase. 816 Mar 46


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