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)

To see whether urine enzyme activities could be used as an index in evaluating the disease status of leukemia patients, we examined the activities of four enzymes: arylsulfatases A(AS-A) and B(AS-B), alkaline phosphatase (AP), and lactate dehydrogenase (LDH). AP and LDH showed no consistent patterns. The activities of AS-A and AS-B correlated well with the patient's clinical status, increasing during progression of disease and decreasing toward normal activities during responses to therapy, as judged from bone marrow cellularity and differential. Among 23 untreated patients with a histologic diagnosis of acute leukemia we found increased activities of the urine enzymes in these proportions: AS-A in 23 patients (100%), AS-B in 22 (95.7%), AP in 7 (30.4%), and LDH in 10 (43.5%). Five patients in remission from acute leukemia had normal activities for all four enzymes. In one patient in remission for more than one year, a rise in urinary arylsulfatase activity preceded observable bone marrow relapse by 4 months. Unlike that of serum of urine lysozyme and serum copper, the determination of urine arylsulfatase activities appears to be a consistent, useful indicator of response to antileukemic therapy. In contrast to the determination of polyamines, the quantitation of arylsulfatase activity is achieved with greater ease and with instrumentation available in most clinical laboratories.
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PMID:A noninvasive technique for monitoring response to chemotherapy in human acute leukemia. 3

Tetrahymena pyriformis strain HSM secretes large quantities of acid hydrolases into the culture medium. An enzyme secreted by the ciliate and capable of degrading walls of streptococci was identified and purified to a considerable degree. The pH optimum of this enzyme was 3--4, and it was eluted after cytochrome c from Sephadex G-75 columns. Unlike lysozyme, the enzyme was thermolabile at pH 2.9, but relatively thermostable at pH 8.1. It degraded 14C-labeled cell walls of streptococci releasing reducing groups. Cell walls prepared from different strains of streptococci differed in susceptibility to this enzyme, the most sensitive strain tested being of group A, type T12. It was shown in immunologic studies that this hydrolase released the group-specific carbohydrate from the walls. Secretions of Tetrahymena from early stationary-phase cultures had more bacteriolytic activity than those from cells from late stationary-phase cultures. Further, cells from cultures grown in glucose-supplemented medium secreted less of the enzyme than ciliates of comparable age grown in unsupplemented proteose-peptone. The newly isolated bacteriolytic enzyme, presumably of lysosomal origin, may be helpful in characterizing streptococcal cell walls.
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PMID:Partial purification and characterization of a bacteriolytic enzyme secreted by Tetrahymena. 3 68

Hen egg white lysozyme has been prepared in which the C epsilon position of the single histidine residue is substituted by a deuterium atom as a nondisturbing stable isotope probe. The deuterium nuclear magnetic resonance (2H NMR) spectrum in H2O shows a broad resonance (500--1000 Hz) due to the histidine deuteron and a sharp signal from residual HOD. The line width of the deuterium signal increases with pH, reflecting the self-association of lysozyme which is known to involve this histidine [shindo, H., Cohen, J.S., & Rupley, J. A. (1977) Biochemistry 16, 3879]. Correlation times calculated from spin-spin relaxation times (T2) derived from the 2H widths indicate that His-15 is restricted in motion and that lysozyme is predominantly dimerized at pH 7.5. Controls carried out with [epsilon-2H]imidazole showed a small pH dependence of the spin-lattice relaxation time (T1), which parallels the 2H chemical shift change upon ionization of the imidazole. Similar results cannot generally be observed by proton nuclear magnetic resonance (1H NMR) because of paramagnetic relaxation due to trace metal ion impurities. The pH dependence of the 2H T1 values indicates a change in the 2H quadrupole coupling constant upon protonation of the imidazole ring.
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PMID:Protein mobility and self-association by deuterium nuclear magnetic resonance. 3 94

The phenotypes of 273 offspring of 56 matings of various genotypes of lysozyme-deficient and normal New Zealand white rabbits were analyzed. It was determined that lysozyme deficiency of rabbits is inherited as an autosomal recessive with complete penetrance. The symbol ld is suggested for the gene for lysozyme deficiency. Further studies on the nature of the condition revealed that the lysozyme deficiency was not due to a lysozyme that was cold labile, or to a lysozyme that was so tightly bound it was unavailable for enzymatic assay, or to a lysozyme with a variant pH optimum. It was demonstrated, however, that the pH profile of the lysozyme remaining in the ld/ld rabbits was different from that found in normal rabbits.
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PMID:Inheritance of lysozyme deficiency in rabbits. 3 55

The previously described temperature and pH-dependent transition in the solid state of hen lysozyme was studied in solution. Experiment concerning the velocity of lysis of M. luteus by lysozyme and its behavior in presence of an inhibitor (GlcNAc) as well as a reinvestigation of the Arrhenius curves over a large range of pH, demonstrated the existence of two temperature-induced domains. An inhibitor-insensitive lysozyme form was characterized at 40 degrees (physiological temperature).
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PMID:The temperature and pH-dependent transition of hen lysozyme. Characterization of two temperature-defined domains and of an N-acetylglucosamine (inhibitor)-insensitive form. 4 Jan 9

Spores of Bacillus cereus T treated with trichloroacetic acid (6.1--61.2 mM) were compared with untreated spores, and as the concentration of the chemical increased, the following alterations in spore properties were found: (1) the extent of germination decreased irrespective of the germination medium used; (2) the spores became sensitive to sodium hydroxide (1 N) and hydrochloric acid (0.27 N), but not to lysozyme (200 micrograms/ml); (3) loss of dipicolinate increased on subsequent heating; and (4) the spores became more sensitive to heat. However, trichloroacetic acid-treated spores were still viable and there was no significant change in spore components. The mechanism of action of trichloroacetic acid is discussed.
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PMID:Effect of trichloroacetic acid treatment on certain properties of spores of Bacillus cereus T. 4 Nov 62

1. A glycol-chitin-splitting enzyme without lysozyme (muramidase) activity has been found in calf serum. The enzyme also degrades colloidal chitin and is thus a true chitinase, 1,4-beta-poly-N-acetylglucosaminidase, without exo-beta-N-acetylglucosaminidase effect. 2. The enzyme is purified 1000-fold by ion-exchange chromatography and gel filtration. Its optimal activity is between pH 1.5-2.0 with glycol chitin and between pH 3-6 in a rather broad optimum with colloidal chitin as substrate. The optimal stability of the enzyme is in the pH interval 3.0-6.5 when tested by incubation with glycol chitin at 50 degrees C for 60 min. The optimal temperature for the degradation of glycol chitin is 40 degrees C when assayed at pH 1.5 and 51 degrees C when assayed at pH 3.5. 3. The enzyme is activated by moderate heating at pH 6.5. The highest relative activity, 135% is reached after 45 min incubation at 30 degrees C, pH 5 or after 30 min at 40, pH 2.4. By incubation with small amounts of trypsin at pH 6.5 at 3m degrees C the enzyme was temporarily activated. 4. The isoelectric point, pH 5.3, and the molecular weight, 47,000 +/- 3,000 were determined by respectively isoelectric focusing and gel filtration. 5. The Michaelis-Menten constant, Km = 0.76 +/- 0.05 (S.E.) mg/ml, was measured with glycol chitin as substrate.
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PMID:Bovine serum chitinase. 4 11

A novel method for the preparation of Kyn 62-lysozyme, in which tryptophan 62 is replaced by kynurenine, is reported. Hen egg-white lysozyme was ozonized in aqueous solution to yield one N'-formylkynurenine residue and deformylated with hydrochloric acid in frozen solution at -10 degrees C. Crude Kyn 62-lysozyme was purified by affinity and Bio Rex 70 chromatography successively. Kyn 62-lysozyme retains affinity for chitin and is essentially an active enzyme with a slightly weakened but distinct catalytic activity. After this modification, the enzyme activity was changed differently depending on the kind of substrate. At the individual optimum pH's, lytic activity was largely retained (80% active), but the catalytic efficiency for hydrolyzing glycol chitin was relatively low (30% active). Lysis of M. lysodeikticus cell suspensions was optimally catalyzed by Kyn 62-lysozyme at pH 6.2 and at 0.088 ionic strength. These values are lower by 1.3 pH unit and 0.04 ionic strength, respectively, than those of intact lysozyme. The optimum pH and ionic strength for the hydrolysis of neutral substrates were scarcely affected. These results suggest the significance of electrostatic interaction in the lysis of lysozyme. Relatively limited loss of activity induced by modification of the 62nd residue, which is thought to participate directly in the binding of the substrate at subsite C, is discussed on the basis of the similarity of side chain structure in tryptophan and kynurenine.
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PMID:Preparation and characterization of an active lysozyme derivative: Kyn 62-lysozyme. 4 44

Ultrastructural and immunohistologic findings in a nodular variant of Hodgkin's disease with lymphocytic predominance, called nodular paragranuloma, are presented and compared with those in so-called progressively transformed germinal centers. These are large follicles with numerous lymphocytes which can be found not only in nonspecific lymphadenitis, but also in lymph nodes from patients with nodular paragranuloma. The immunoperoxidase technique was applied on paraffin sections to detect intracytoplasmic immunoglobulin and lysozyme. The so-called L & H type Sternberg-Reed cells contained IgG and one type of light chain per cell, suggesting that such cells produce immunoglobulin. The ultrastructure of the L & H type Sternberg-Reed cells favored the immunoblastic nature of these cells. It is concluded that nodular paragranuloma differs from other types of Hodgkin's disease by its localization in B-cell areas and the presence of atypical B immunoblasts.
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PMID:Nodular paragranuloma and progressively transformed germinal centers. Ultrastructural and immunohistologic findings. 4 15

30 patients on long-term lithium therapy have been studied. The results are presented of the urinary concentrating ability after water deprivation and the intranasal administration of vasopressin, of the simultaneous determination of glomerular filtration rate (GFR) and effective renal plasma flow (ERPF), of the minimal urine pH after an oral dose of ammonium chloride, and of the urinary beta-2-microglobulin excretion. Mean urine concentration (+/- SEM) after 22 hr water deprivation (= Uosm) amounted to 854 +/- 22 mOsm/kg H2O, mean GFR was 101 +/- 4 ml/min, mean ERPF 360 +/- 18 ml/min, and mean minimal urine pH 4.95 +/- 0.06. In 8 out of 30 patients there was polyuria. In these 8 patients the values were 778 +/- 51 mOsm/kg H2O, 113 +/- 6 ml/min, 415 +/- 33 ml/min and 4.99 +/- 0.08, respectively. Serum levels of beta-2-microglobulin and lysozyme and the urinary excretion of beta-2-microglobulin were normal in all patients. No correlation was established between Uosm and the serum lithium concentration during the test (0.8 +/- 0.05 mmoles/l) nor between Uosm and the average serum lithium level during treatment (0.79 +/- 0.03). GFR was only correlated with age. It was found that administration of indomethacin during the concentration test increased Uosm in these patients. The results suggest that, given proper dosage and surveillance, long-term treatment with lithium is not likely to cause disturbances in renal function.
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PMID:A renal function study in 30 patients on long-term lithium therapy. 4 7


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