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)

The distribution of lysozyme, alkaline phosphatase, aminopeptidase, maltase and amylase was studied throughout the small intestine of the adult rat. Lysozyme activity increases along the length of the small intestine and the behaviour of this enzyme slightly differs from the mucosal enzymes reported in this investigation. A positive correlation is found between the percentage of crypts with granulated Paneth cells and the lysozyme activity. This corroborates with the secretory origin of this enzyme from these intestinal cells.
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PMID:The quantitative distribution of certain enzymes along the small intestine of the rat and its correlation with the villous area and the Paneth cells. 35 72

The influence of moderate malnutrition on immunoglobulins and enzymes in the sera and secretions of 71 Colombian children was studied. Concentrations of immunoglobulin A, immunoglobulin G, lysozyme, albumin, and aminopeptidase were measured in the sera, tears, and saliva of 27 normal, 32 grade I, 9 grade II, and 3 grade III malnourished children. The most severely malnourished children, grades II and III, had markedly reduced immunoglobulin A concentrations and elevated immunoglobulin G concentrations in tears. Immunoglobulin A levels in whole saliva were also reduced in these malnourished children. In contrast, the concentration of immunoglobulin A in the sera of these children was significantly elevated. There was no influence of malnutrition on levels of lysozyme, albumin, total protein, and aminopeptidase in tears or saliva. These results indicate that secretory immunity may be impaired in moderately malnourished children due to decreased levels of immunoglobulin A in secretions.
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PMID:Effect of moderate malnutrition on concentrations of immunoglobulins and enzymes in tears and saliva of young Colombian children. 93 Aug 66

Removal of just the three N-terminal residues Lys-Val-Phe (TIP) on hen egg white lysozyme (HEL), by aminopeptidase cleavage, eliminates an antigenic determinant which is a recurrent and dominant focus of primary but not secondary antibody responses to HEL in a variety of mouse strains. We have generated an anti-idiotypic rabbit antiserum against such a TIP-dependent monoclonal antibody (mAb). This antiserum reacts with many different primary anti-HEL mAb, but fails to react with all of a variety of secondary anti-HEL mAb. The idiotype defined by this antiserum, termed IdXE, is a common feature of early anti-HEL antibody responses but does not appear in secondary responses. Although the presence of IdXE and TIP dependence is correlated in primary responses, studies of idiotype expression on mAb and on plaque-forming cells (PFC) using mixed erythrocyte monolayers clearly show that at the single-cell level the properties are separable, i.e., not all TIP-recognizing PFC display IdXE and a sizable proportion of cells producing non-TIP-dependent antibodies are IdXE+. The restricted idiotypy and specificity of early antibody responses to HEL occur in each of eight diverse mouse strains tested: it is not associated with a particular MHC haplotype, heavy chain allotype or light chain allotype. The finding of such strain-independent restriction in the early response pattern to a typical protein antigen is novel and suggests the involvement of highly conserved, potent regulatory mechanisms which are manifested as a limitation in the initial expression of the available repertoire.
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PMID:A predominant idiotype independent of specificity, or Ig and H-2 allotypes, is found in the primary but not the secondary murine antibody response to lysozyme. 246 7

The activity levels of serum acid phosphtase, aminopeptidase, and lysozyme in a Brazilian strain of Biomphalaria glabrata were ascertained at 1, 2, and 3 hr after mechanical wounding or injection with albumin on the 30th day postexposure to a compatible strain of Schistosoma mansoni miracidia and found to be elevated. Parallel transmission electron microscope studies on daughter sporocysts and developing cercariae at these time intervals revealed progressive disintegration of the parasites that was associated with increased numbers of host granulocytes abutting the sporocyst surfaces. Furthermore, host granulocytes were observed to have passed through eroded sporocyst walls and attacked developing cercarial embryos. It is proposed that the elevated levels of lysosomal hydrolases released from activated host granulocytes as a result of challenge altered the parasite's surfaces so that these were recognized as nonself. Consequently, additional host granulocytic response, which included additional release of lysosomal enzymes into serum as well as phagocytosis of remnants of both sporocysts and developing cercariae, was elicited.
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PMID:Ultrastructural evidence for the destruction of Schistosoma mansoni sporocysts associated with elevated lysosomal enzyme levels in Biomphalaria glabrata. 261 3

The lysozyme-induced fusion of phosphatidylserine/phosphatidylethanolamine vesicles as studied at a wide range of pH is found to correlate well with the binding of this protein to the vesicles. An identical 6000 molecular weight segment of lysozyme at the N-terminal region is found to be protected from tryptic digestion when initially incubated with vesicles at several pH values. Only this segment is labeled by dansyl chloride, which is partitioned into the bilayer. These results suggest the penetration of one segment of lysozyme into the bilayer. Photoactivated labeling of the membrane-penetrating segment of lysozyme with 3-(trifluoromethyl)-3-([125I]iodophenyl)diazirine ([125I]TID) and subsequent identification of the labeled residues by Edman degradation and gamma-ray counting indicate that four amino acids from the N-terminal are located outside the hydrophobic core of the bilayer. Although treatment of the membrane-embedded segment with aminopeptidase failed to cleave any amino acids from the N-terminal, it appears that a loop of lysozyme segment near the N-terminal penetrates into the bilayer at acidic pH. A helical wheel diagram shows that the labeling is done mainly on one surface of the alpha-helix. The penetration kinetics as studied by time-dependent [125I]TID labeling coincide with the fusion kinetics, strongly suggesting that the penetration of the lysozyme segment into the vesicles is the cause of the fusion.
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PMID:Penetration and fusion of phospholipid vesicles by lysozyme. 277 69

A urinary enzyme pattern consisting of two lysosomal enzymes, N-acetyl-beta-glucosaminidase and lysozyme, and one enzyme originating from kidney tubular brush border membrane, alanine-aminopeptidase, were studied in 30 patients undergoing intravenous urography and arteriography. N-acetyl-beta-glucosaminidase and lysozyme showed the greatest diagnostic sensitivity and were still abnormal on the fifth day after the administration of radio contrast agent. The results, which are statistically significant (Student's t test), suggest that radio-contrast agents are potentially nephotoxic.
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PMID:Variation of urinary enzymes N-acetyl-beta-glucosaminidase, alanine-aminopeptidase, and lysozyme in patients receiving radio-contrast agents. 289 55

Forty-three workers exposed to low levels of toluene diisocyanate (TDI) during the process of producing polyurethane forms were examined immunologically for IgG, A, M, and E and serum enzyme activities such as serum angiotensin converting enzyme (SACE), serum lysozyme (SLZM) and glycylproline dipeptidyl aminopeptidase (GP-DAP). Air concentration of TDI was annually measured in various places of work during the past five years from 1979 to 1983. The results obtained in the present study were as follows. 1. The air concentration of TDI at all places of work was below the permissible concentration level of 0.02 ppm throughout the study period. 2. Subjective symptoms and abnormal findings on chest X-ray considered directly related to TDI exposure were not observed. 3. No remarkable abnormal findings in blood cell counts and in serum biochemical studies could be seen in any of the workers. 4. The serum IgG levels in workers directly exposed to TDI were significantly higher (p less than 0.05) than those in workers indirectly exposed to TDI and in non-exposed workers. 5. In the study of serum enzymatic activity, SLZM activity in workers exposed directly to TDI was significantly higher (p less than 0.01) than those in workers indirectly exposed to TDI and in non-exposed workers.
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PMID:[A study on the immunologic effects in workers exposed to low levels of toluene-diisocyanate (TDI)]. 304 Oct 74

The efficacy, renal effects and nephrotoxicity of a short course of treatment with azthreonam were evaluated in 11 adult patients with urinary tract infection. Azthreonam was administered for 5 days at a daily dose adjusted to the residual renal function of the patients. In the pre-treatment period, during treatment and 10 days after completion of therapy, urine cultures, urinalysis and routine renal function tests (clearance of creatinine, urea and uric acid) were performed and urinary enzymes (alanine-aminopeptidase, gamma-glutamyl-transpeptidase, N-acetyl-beta-D-glucosaminidase, lysozyme) were determined. Renal haemodynamics (glomerular filtration rate and effective renal plasma flow) were measured in the pretreatment period and on the 5th day of therapy. The results confirm the efficacy of azthreonam for treatment of urinary tract infection. Results of renal function tests and measurements of urinary enzymes remained unchanged during and after treatment with azthreonam. These data support the conclusion that azthreonam is an effective antimicrobial agent which does not influence renal function or cause nephrotoxic effects.
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PMID:Azthreonam in the treatment of urinary tract infection: evaluation of efficacy, renal effects and nephrotoxicity. 362 45

In a survey the present state of the activity determination of urinary enzymes after kidney transplantation as a diagnostic tool in the control of patients with transplanted kidney is described. A great number of enzymes has up to now been established in these patients. The most extensive data are present for the enzymes alanine-aminopeptidase, N-acetyl-beta-D-glucosaminidase and lysozyme. After the transplantation of the kidney typical excretion patterns of the enzymes in the urine are observed in immediate function, retarded onset of the function, without function and acute rejection of the graft. Particularly the behaviour of the urinary enzyme excretion during acute rejection reactions can be diagnostically used. Hereby, the diagnostic reliability of determinations of the activity of urinary enzymes is, however, differently assessed by various authors. In future works in close cooperation between clinic and laboratory the diagnostic validity of the determinations shall unambiguously be characterized and the determinations of the enzyme activity in the urine should be summarized together with other parameters to an optimum combination of parameters for the follow-up investigation of patients who underwent kidney transplantation.
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PMID:[Urinary enzyme excretion in kidney transplant patients]. 614 71

The lack of response to hen egg white lysozyme (HEL) by C57BL (H-2b) mice has been demonstrated previously to be related to the induction of suppressor T (Ts) cells which recognize the amino terminal region of HEL. In this report, the nature of the protein determinant required for Ts cell induction is more precisely detailed using des-1,2,3-HEL (AP-HEL) prepared with an aminopeptidase purified from Aeromonas proteolytica . Remarkably, the removal of just these three amino acids obliterates the ability of HEL to induce Ts cells specific for HEL. Additionally, in contrast to HEL, AP-HEL is able to prime for an in vitro T cell proliferative response to either AP-HEL or HEL. Thus, removal of a very limited region of a protein antigen can drastically alter its immunogenic properties.
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PMID:Immunodominant protein epitopes. I. Induction of suppression to hen egg white lysozyme is obliterated by removal of the first three N-terminal amino acids. 620 28


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