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:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Yellow-brown bodies were observed in the sinusoids of lymph node and histiocytes. The authors confirmed immunohistochemical reactivity of lysozyme, alpha-1-antichymotrypsin, S-100 protein, alkaline phosphatase, and acid phosphatase in non-phagocytic and phagocytic histiocytes which contained yellow-brown bodies. Phagocytic histiocytes (histiocytes with yellow-brown bodies) were not reacted with lysozyme, alpha-1-antichymotrypsin, S-100 protein, alkaline phosphatase, and acid phosphatase. On the other hand, non-phagocytic histiocytes were reacted with lysozyme, alpha-1-antichymotrypsin, S-100 protein, alkaline phosphatase, and acid phosphatase.
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PMID:Immunohistochemical reactivity of phagocytic and non-phagocytic histiocytes in lymph nodes with lysozyme, alpha-1-antichymotrypsin, S-100 protein, alkaline phosphatase, and acid phosphatase. 281 76

Rat neutrophils added to 3H-labelled glomerular basement membrane (GBM) treated with rabbit anti-rat GBM antiserum degraded the GBM as judged by the release of 3H-labelled peptides. Cells from female animals promoted a more marked degradation than cells from males. This correlated with measurements of higher levels of elastase in granule fractions from the cells. The subcellular distributions of granule marker enzymes was found not to differ between the sexes. Levels of myeloperoxidase, lysozyme, cathepsin G, alkaline phosphatase, gamma-glutamyltranspeptidase and N-acetyl-beta-glucosaminidase showed no sex-based differences. No alpha-mannosidase could be detected in the cells.
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PMID:Biochemical studies of neutrophils from male and female rats: a differential response to basement membrane treated with nephrotoxic antiserum. 284 4

We compared the diagnostic validity of five urinary enzymes--alanine aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), gamma-glutamyltransferase (EC 2.3.2.2), N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30), and lysozyme (EC 3.2.1.17)--as indicators of acute rejection crises in renal-transplant recipients. In 82 patients (group A), the excretion of each of these five enzymes was measured daily from transplantation until discharge from hospital. In another 69 patients (group B), enzyme determinations were made when the patient came for regular checkups (about every four to eight weeks). We used an "activity ratio" (the activity measured at a particular time compared with the activity on the preceding determination) value of 1.5 as the decision point. In group A, use of this discrimination point for alanine aminopeptidase, gamma-glutamyltransferase, and N-acetyl-beta-D-glucosaminidase yielded a specificity and sensitivity of about 90%. In group B, only alanine aminopeptidase had a greater diagnostic sensitivity than creatinine alone. Evidently, measurement of alanine aminopeptidase can be a helpful indicator of acute rejection crises, when interpreted in combination with other available relevant clinical, biochemical, and immunological data.
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PMID:Diagnostic significance of some urinary enzymes for detecting acute rejection crises in renal-transplant recipients: alanine aminopeptidase, alkaline phosphatase, gamma-glutamyltransferase, N-acetyl-beta-D-glucosaminidase, and lysozyme. 287 13

We examined the stability of N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30), alanine aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), gamma-glutamyltransferase (EC 2.3.2.2), and lysozyme (EC 3.2.1.17) in urine prepared by gel filtration and supplemented with albumin, or ethylene glycol, or ethylene glycol plus albumin during storage at -20 degrees C for a period of 12 months. The stability was assessed by linear regression analysis of monthly values versus time. All enzymes except for gamma-glutamyltransferase could be considered stable for about one year in all three control materials provided that maximum change of 10% of the starting enzyme activity is accepted as tolerable. If ethylene glycol is used as stabilizer, its suitability must be tested and its inhibitory effect on enzyme activities must be taken into account in intermethod comparisons, because in some methods, it may be removed in a pretreatment step.
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PMID:Quality control material for activity determinations of urinary enzymes. 289 58

We measured the excretion rates of six urinary enzymes that either originate from the proximal renal tubule, like alanine aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), gamma-glutamyltransferase (EC 2.3.2.2), and N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30), or that are typical low-molecular-mass proteins, like lysozyme (EC 3.2.1.17) and pancreatic ribonuclease (EC 3.1.27.5). These rates were compared with those of total protein and albumin in urine of 36 insulin-dependent diabetic men and 30 healthy men. Seventeen of the diabetics had "clinical proteinuria," defined as excretion of more than 7.5 g of protein per mole of urinary creatinine (group B). Group A comprised the 19 diabetics without proteinuria. Except for gamma-glutamyltransferase, the excretions of enzymes and proteins were significantly higher in diabetics than in controls and were greater in group B than in group A. N-Acetyl-beta-D-glucosaminidase was the analyte most often increased in group A (89%), followed by albumin and alkaline phosphatase (each 32%). All patients in group B showed increased excretion of N-acetyl-beta-D-glucosaminidase. We conclude from the comparative data that this enzyme may be useful as an early predictor of diabetic nephropathy.
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PMID:Urinary enzymes and low-molecular-mass proteins as indicators of diabetic nephropathy. 289 6

The C-terminal two-thirds of the rat liver ATP synthase beta subunit has been overexpressed and exported to the Escherichia coli periplasm under the direction of the alkaline phosphatase (phoA) promoter and leader peptide. The processed soluble protein contains the 358 amino acids from glutamate 122 to the rat liver beta C-terminal serine 479, including all the regions that have been predicted by chemical and genetic modification studies to be involved in nucleotide, Pi, and Mg2+ binding. Through a simple sequence of Tris/EDTA/lysozyme treatment, osmotic lysis, and alkaline pH washes, the processed beta subunit fragment can be prepared in greater than 95% purity and at a yield of greater than 20 mg/liter of culture. It interacts with 2'(3')-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP) which exhibits a strong enhancement of fluorescence upon binding. A similar enhancement is observed upon interaction with TNP-ADP. Enhancement observed with both TNP-nucleotides is markedly reduced by prior addition of either ATP or ADP and almost completely prevented by the ATP synthase inhibitor 7-chloro-4-nitrobenz-2-oxa-1,3-diazole. Both TNP-ATP and TNP-ADP bind at a stoichiometry of approximately 1 mol of nucleotide/mol of beta subunit fragment. Under the same conditions, TNP-AMP does not exhibit a fluorescence enhancement. This work demonstrates that, in the absence of interaction with other ATP synthase subunits, the rat liver beta subunit sequence from glutamate 122 to the C terminus exhibits no more than one readily detectable nucleotide binding domain. This success in producing a "functional" beta subunit fragment has significance for the pursuit of genetic and physical studies focused on the structure and function of the rat liver ATP synthase beta subunit.
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PMID:Mitochondrial ATP synthase. Overexpression in Escherichia coli of a rat liver beta subunit peptide and its interaction with adenine nucleotides. 290 92

Extramedullary tissue infiltrates of acute myeloid leukemia are rare and often difficult to recognize in routine paraffin-embedded tissue sections. Since appropriate therapy for these tumors depends on their precise identification, we have studied a series of tissues infiltrated with primitive myeloid cells using monoclonal and polyclonal antibodies capable of labeling cells of the myeloid/monocytic system in paraffin-embedded tissue sections. The current retrospective study involved tissues from 15 patients (eight men and seven women) with a mean age of 51 years (range, 23-77). A diagnosis of extramedullary myeloid cell tumors had been made on the basis of routine histology, chloroacetate esterase cytochemical stain, and--in some cases--electron microscopy. Paraffin-embedded tissue sections were cut and stained employing the alkaline phosphatase antialkaline phosphatase (APAAP) immunocytochemical procedure with monoclonal antibodies against leukocyte-common antigen (PD7/26-2B11), restricted components of the leukocyte-common antigen (UCHL1, 4KB5), granulocytes (Mac-387, Leu-M1), leukocytes (MT1, MT2, LN1, LN2), HLA-DR (LN3), and elastase (NP57), as well as polyclonal antibodies against lactoferrin, lysozyme, alpha-1-antitrypsin, and alpha-1-antichymotrypsin. Results indicate that antibodies against Mac-387, elastase, and lysozyme are most useful in the recognition of neoplastic myeloid cells. We conclude that tissues containing granulocytic tumors can be identified in paraffin-embedded tissue sections using a panel of antibodies and the APAAP procedure.
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PMID:The immunophenotyping of extramedullary myeloid cell tumors in paraffin-embedded tissue sections. 297 Aug 8

Avidin-biotin technology has been employed for the improved nonradioactive detection of glycoproteins on blots. Periodate oxidation of samples on blots converts the glycoprotein-based carbohydrate residues to the corresponding aldehydes. The latter undergo interaction with preformed complexes consisting of either avidin hydrazide or streptavidin hydrazide combined with biotinylated alkaline phosphatase. The sensitivity of the new assay exceeds the previously described enzyme hydrazide method by a factor of at least 10. The approach can be rendered selective for sialoglycoproteins, and approximately 12 sugar-containing bands could be observed in erythrocyte membrane preparations. Problems of nonspecific binding and high levels of background label were alleviated using a nonglycosylated basic protein (lysozyme) for quenching.
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PMID:Enzyme-based detection of glycoproteins on blot transfers using avidin-biotin technology. 303 95

Nourseothricin (streptothricin) causes disturbances (perforations) in the outer membrane of sensitive E. coli strains allowing lysozyme and deoxycholate, but not the periplasmic alkaline phosphatase to penetrate. EDTA slightly increases, but Mg++ ions slightly decrease this effect. The cell walls of three from four nourseothricin-resistant strains do not become permeable under these conditions, but remain sensitive against TRIS/EDTA. Nourseothricin is supposed to pass the outer membrane of sensitive bacteria via some kind of "self-promoting" pathway. This way can (but need not) be blocked in resistant strains.
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PMID:Effect of nourseothricin (streptothricin) on the outer membrane of sensitive and resistant Escherichia coli strains. 304 Sep 61

Streptococcus faecalis S-48 produces a broad spectrum antibiotic, active against Gram-positive and Gram-negative bacteria. This substance is produced in solid and liquid media and also in a defined basal medium. It is sensitive to protease, pronase, or trypsin, heating at 70 degrees C, and alkaline pH, but resistant to treatment with lipase, lysozyme, alkaline phosphatase, DNAase, RNAase, acidic or neutral pHs, and also lower temperatures (60 degrees C). Several organic solvents cause precipitation, but not inactivation. This antibiotic has been partially purified by gel filtration and further ion-exchange chromatography. Its molecular weight has been estimated close to 2000. The biological activity of this antagonistic substance against the selected indicator strains, Streptococcus faecalis S-47 and Escherichia coli U-9, is bactericidal. The characterization of this substance, initially classified as a bacteriocin, indicates that it is an antibiotic of peptidic nature. The significance of antibiotic occurrence in group D of the genus Streptococcus is also discussed.
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PMID:Characterization and partial purification of a broad spectrum antibiotic AS-48 produced by Streptococcus faecalis. 309 96


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