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)

Paraffin sections of formaldehyde-fixed renal biopsies were labeled for complement C3 by a polyclonal rabbit antibody to human complement C3, by the peroxidase-antiperoxidase complex (PAP) and the avidin-biotin peroxidase complex (ABC) techniques, respectively. All tissues had C3 deposits according to direct immunofluorescence on fresh frozen sections. Staining for muramidase was introduced as an intrinsic control for the degree of tissue proteolysis after the necessary trypsin digestion prior to the immunoenzyme labeling. The results indicated that even minute deposits of C3 could be detected in paraffin sections by the ABC method, which was more sensitive than the PAP technique; the ABC method allowed a maximal dilution of 1:2,400 of the primary antibody as compared to 1:800 for the PAP technique.
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PMID:Conditions for the immunohistochemical demonstration of complement factor C3 in formaldehyde-fixed and paraffin-embedded renal tissues. 242 Jul 64

The cellular sediments of 42 malignant and 16 benign effusions (58 cases) were studied using the immunoperoxidase technique. Serial sections of formalin-fixed, paraffin-embedded residual sediments of effusions, sent for routine cytologic examination, were studied by commercially available polyclonal antisera against lysozyme, alpha 1-anti-trypsin, alpha 1-anti-chymotrypsin, tissue polypeptide antigen (TPA), a wide-spectrum anti-keratin, carcinoembryonic antigen (CEA) and, in single cases, thyroglobulin and prostate-specific antigen. A final definite diagnosis from histologic study of biopsy or autopsy specimens was known in all cases. All carcinomas, the mesotheliomas and the reactive mesothelial cells showed a positive reaction for TPA and, partly, the wide-spectrum keratin. Lysozyme could be demonstrated in the cells of the one proven malignant fibrous histiocytoma; all malignant epithelial cells were negative. Alpha 1-anti-chymotrypsin and alpha 1-anti-trypsin showed similar reactions: they were often positive in carcinoma cells of the breast, the bronchial system and the pancreas, in contrast to a mostly negative reaction in carcinomas of the stomach and ovary. CEA showed considerable differences; it was always negative in benign and malignant mesothelial proliferations but mostly positive in carcinomas of the stomach, pancreas and bronchial system. It was only positive in less than 20% of the carcinomas of the breast and always negative in the proven malignant effusions of primary carcinomas of the ovary and prostate. Studying a combination of several tumor markers is possible in serial paraffin-embedded sections and may be a valuable criterion in the cytologic diagnosis of effusions.
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PMID:Immunohistochemical study of lysozyme, alpha 1-anti-chymotrypsin, tissue polypeptide antigen, keratin and carcinoembryonic antigen in effusion sediments. 243 1

Gastro-intestinal mucosa obtained at surgical resection was studied by light microscopy using the unlabelled antibody enzyme method for immunohistochemical staining of lysozyme, anionic trypsin, cationic trypsin and pancreatic trypsin inhibitor (PSTI). Paneth cells, identified by their content of lysozyme, contained anionic trypsin, cationic trypsin and PSTI-like immunoreactivity. The demonstration of immunoreactive trypsin and immunoreactive PSTI is a further indication of the resemblance between Paneth cells and the pancreatic acinar cells.
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PMID:Immunohistochemical demonstration of pancreatic secretory proteins in human paneth cells. 243 86

A monoclonal antibody was used to characterize a serogroup 1 specific Legionella pneumophila Philadelphia strain 1 antigenic determinant. A quantitative fluorometric assay was developed to quantitate the antibody sites (2.7 +/- 0.4 X 10(5)) on Legionella bacteria and to determine the physico-chemical parameters of the antibody-antigen interaction (at 4 degrees C: delta G = -10.9 Kcal X mol-1, delta H = 1.7 Kcal X mol-1, delta S = 45 cal X K-1 X mol-1). The same method was used to study the modification or the removal of the antigen by chemical and enzymatic means (trypsin, papain, lysozyme, acetone, chloroform-methanol and Tris-EDTA); only Tris-EDTA extraction resulted in a significant decrease in antibody binding sites. Inhibition studies of the fluorescein-labelled antibody binding were performed with different sugars of which only L-fucosylamine was inhibitory, and with other monoclonal antibodies to Legionella pneumophila serogroup 1 in order to compare their fine specificity and affinity. The results indicate that the epitope recognized was an immunodominant carbohydrate including an aminodideoxyhexose and carried by the lipopolysaccharide.
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PMID:Partial characterization of a Legionella pneumophila serogroup 1 immunodominant antigenic determinant recognized by a monoclonal antibody. Legionella specific antigenic determinant. 243 83

Solvent exchange of 18O-labeled buried water in bovine pancreatic trypsin inhibitor (BPTI), trypsin, and trypsin-BPTI complex is measured by high-precision isotope ratio mass spectrometry. Buried water is labeled by equilibration of the protein in 18O-enriched water. Protein samples are then rapidly dialyzed against water of normal isotope composition by gel filtration and stored. The exchangeable 18O label eluting with the protein in 10-300 s is determined by an H2O-CO2 equilibration technique. Exchange of buried waters with solvent water is complete before 10-15 s in BPTI, trypsin, and BPTI-trypsin, as well as in lysozyme and carboxypeptidase measured as controls. When in-exchange dialysis and storage are carried out at pH greater than or equal to 2.5, trypsin-BPTI and trypsin, but not free BPTI, have the equivalent of one 18O atom that exchanges slowly (after 300 s and before several days). This oxygen is probably covalently bound to a specific site in trypsin. When in-exchange dialysis and storage are carried out at pH 1.1, the equivalent of three to seven 18O atoms per molecule is associated with the trypsin-BPTI complex, apparently due to nonspecific covalent 18O labeling of carboxyl groups at low pH. In addition to 18O exchange of buried waters, the hydrogen isotope exchange of buried NH groups H bonded to buried waters was also measured. Their base-catalyzed exchange rate constants are on the order of NH groups that in the crystal are exposed to solvent (static accessibility greater than 0) and hydrogen-bonded main chain O, and their pH min is similar to that for model compounds. The pH dependence of their exchange rate constants suggests that direct exchange with water may significantly contribute to their observed exchange rate.
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PMID:Solvent exchange of buried water and hydrogen exchange of peptide NH groups hydrogen bonded to buried waters in bovine pancreatic trypsin inhibitor. 244 53

Proteolytic enzymes were tested for improving histochemical localization of tissue antigens. Sections, 2-4 micron in thickness, were prepared on sodium-silicate coated slides from formalin-fixed, paraffin-embedded human biopsies. A modification of the Sternberger technique (PAP) and the indirect immunofluorescence method were used for the localization of 15 various antigens: heavy chain immunoglobulins, light chain immunoglobulins, alpha 1-fetoprotein, alpha 1-antichymotrypsin, myoglobin, fibronectin, factor VIII (ass. ag), fibrinogen, lysozyme and cytokeratin. The ability of different proteolytic enzymes (trypsin, pronase, pepsin) to unmask antigen in formalin-fixed sections were tested by variation of concentration, incubation time, temperature and pH. Although proteolytic unmasking to some extent is reliable, good restoration of antigenicity is not always possible. Best results were obtained with pronase E (Serva, FRG).
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PMID:[The proteolytic pretreatment of formalin-fixed tissue in immunohistochemical diagnosis]. 245 12

The purpose of this work was to investigate the relationship between rotavirus infection, diagnosed in faeces using the serological test, in calves with diarrhoea and the activity of lysozyme, alpha-amylase, lipase and trypsin in the same material. The faeces were taken from 28 sick and 1 healthy animals, aged from 1 to 5 days, for microbiological and enzymatic examination. No correlation was found between lysozyme activity in faeces and rotavirus infection. Similar results were obtained with the other enzymes.
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PMID:Rotavirus infection in newborn calves. I. Evaluation trials of certain enzymes in faeces. 246 66

Local protection in patients with complicated tuberculosis was investigated. The bronchoalveolar lavage fluid (BALF) was tested for the levels of IgA, sIgA, IgM, IgG, lysozyme, activity of granulocyte proteinases (elastase and trypsin-like proteinases) and their acid-fast inhibitors, ability to produce interferons by the BALF cells, the BALF cell composition and functional activity of alveolar macrophages. The local protection was shown to be decreased in the patients with nonspecific inflammatory processes in the bronchi. The decrease was especially pronounced in the patients with purulent endobronchitis. The data indicated the necessity of using immunocorrectors in combined therapy of such patients.
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PMID:[Bronchopulmonary local defense in nonspecific endobronchitis in patients with tuberculosis]. 247 69

Liquid-liquid protein extraction with reverse micelles is a new method for protein separation. We studied the effects of pH, ionic concentration, cation type, and protein molecular mass on performance of an AOT/isooctane reverse micelle system in extraction of lysozyme, trypsin, and pepsin. Extraction was found to be very efficient for low-molecular-mass proteins.
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PMID:Protein extraction with reverse micelles. 249 28

Soluble reduced lysozyme was extensively digested by a trypsin-like protease purified from the culture supernatant of the bacterium. The digestion peptides were separated and purified by reversed-phase high-performance liquid chromatography, and were subjected to amino acid analysis. The fragments were identified by their amino acid composition, and the cleavage sites in the lysozyme chain were determined. Like mammalian trypsin, the enzyme from B. gingivalis split peptide bonds non-specifically at carboxyl sides of internal arginine and lysine residues, but the lysine present at the amino terminus of the lysozyme chain was not released. In addition, the enzyme cleaved the peptide linkage at the amino side of lysine and bonds between leucine-glycine, alanine-leucine and leucine-serine. Thus the trypsin-like protease from B. gingivalis has some cleavage actions on lysozyme different from those of mammalian trypsin.
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PMID:Cleavage action of a trypsin-like protease from Bacteroides gingivalis 381 on reduced egg-white lysozyme. 251 80


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