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)

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

The main pathological feature of experimental legionellosis produced by the intraperitoneal inoculation of guinea-pigs was a fibrinopurulent peritonitis, especially over the liver and spleen. Foci of necrosis were present in these organs from the second to seventh day after infection. Early biochemical changes in the serum included significant decreases in the concentration of zinc and iron, and increases in copper and triglycerides. Phenylalanine to tyrosine ratios increased strikingly, but free amino acid decreased slightly. The total protein concentration did not change, but acute-phase proteins increased. Serum lysozyme activity increased as leucocytosis developed but fell during the subsequent leucopenia. In the later stages of the disease the activity of alkaline phosphatase, gamma-glutamyl transpeptidase, and creatine kinase decreased; that of dehydrogenases and transaminase increased.
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PMID:Pathological and biochemical features of Legionella pneumophila infection in guinea-pigs. 712 Mar 55

A gamma-glutamyl peptide-hydrolysing enzyme was partially purified from Actinobacillus actinomycetemcomitans. The enzyme required metal ions, and 1 to 2 mM Mn2+ ions, especially, were essential for hydrolytic reaction. Its distribution by treatment of cells with lysozyme-EDTA suggested that the enzyme was a membrane-bound protein. The pI of the enzyme was in range of pH 5.1 to 5.6, and the apparent Km value for gamma-glutamyl-p-nitroanilide was 3.0 x 10(-4) M. The enzyme hydrolysed specifically gamma-glutamyl residues from the N-terminal of gamma-glutamyl compounds such as gamma-Glu-Met, gamma-Glu-Ala, gamma-Glu-Leu and gamma-Glu-Tyr, but did not catalyse the transpeptidation reaction. Neither free amino acids such as Ala-, Pro-, Gly- and Leu-p-nitroanilide nor alpha-glutamyl derivatives were hydrolysed. Its activity was strongly inactivated by metal chelators (EDTA or o-phenanthroline) and amino acids (Glu, Gln). In addition, the activity was specifically inactivated by gamma-glutamyl affinity-labelling reagents such as AT-125, 6-diazo-5-oxo-L-norleucine and azaserine, which are inhibitors of the gamma-glutamyl donor sites of mammalian gamma-glutamyl transpeptidase. Antibodies against bovine kidney gamma-glutamyl transpeptidase decreased the activity of the bacterial enzyme by 65%. These results suggested that the active sites in the bacterial enzyme were similar to those in mammalian gamma-glutamyl transpeptidase.
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PMID:Partial purification and some properties of gamma-glutamyl peptide-hydrolysing enzyme from Actinobacillus actinomycetemcomitans. 779 32

A series of chromatographic techniques was used to purify gamma-glutamyl transpeptidase from Fusobacterium nucleatum ATCC 23726. The purified enzyme was homogenous with a molecular weight (MW) of approximately 101 kD consisting of two different subunits with MW of 67 kD and 31 kD. Its distribution by treatment of lysozyme-EDTA suggested that the enzyme was a periplasmic protein. The pl of the enzyme was 5.9 to 6.2, and the optimum pH of the transpeptidation and the hydrolytic reaction was 8.0. Glycylglycine, glycine and methionine were good acceptors, and the enzyme reaction, in the presence of glycylglycine, was especially efficient. Glutamic acid, glutamine and serine were poor acceptors, and the enzyme activity was inhibited by these amino acids. The apparent Km value for the gamma-glutamyl donor (gamma-glutamyl-p-nitroanilide) was 4.9 x 10(-4)M and that for the acceptor (glycylglycine) was 0.19 M. Affinity-labelling reagents, such as DON, azaserine and AT-125 strongly inhibited the enzyme activity, and its activity was inhibited by L-serine plus borate, as is mammalian gamma-glutamyl transpeptidase. The antibodies against gamma-glutamyl transpeptidase from bovine kidney reduced the activity of the bacterial enzyme by 65%. These results indicate that the catalytic sites in F. nucleatum gamma-glutamyl transpeptidase were similar to those in mammalian gamma-glutamyl transpeptidase.
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PMID:Some properties of gamma-glutamyl transpeptidase from Fusobacterium nucleatum. 941 37


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