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)

We investigated protein accumulation on disposable extended wear contact lenses. Fifteen volunteers were fit with one low water content, non-ionic lens (Bausch & Lomb's SeeQuence) randomly assigned to one eye and a high water content ionic lens (Vistakon's Acuvue) assigned to the fellow eye. During the first 7 weeks of extended wear the lenses were removed weekly for sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of protein deposition, and replacement lenses were inserted. Four subjects completed additional test sessions of 1 minute, 15 minutes, 24 hours, and 1 week extended wear. Lysozyme accumulation, as measured by SDS-PAGE, increased with wearing times up to one week on all Acuvue lenses, but after 24 hours wear lysozyme accumulation did not increase on the SeeQuence lens. Proteins falling into the reported molecular weight ranges of albumin, PMFA, IgG, IgA (sec), lactoferrin and subunits of protein G were evident on all gels at 1 minute of wear, but these protein groups did not have a detectable increase in deposition after 24 hours wear for either the SeeQuence or the Acuvue lenses. In most cases, the protein accumulation evident from SDS-PAGE analysis was not observable by biomicroscopy using standard clinical methods. A few patients reported preference for the initial comfort and vision achieved by the Acuvue lens, but no preference was found after adaptation.
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PMID:Protein accumulation on disposable extended wear lenses. 200 85

A comparison of the efficiencies of hydrophobic interaction chromatography, ion-exchange chromatography, reversed-phase chromatography and gel permeation chromatography in the separation of tear proteins was made using a variety of different buffers. Separation of immunoglobulins, lactoferrin, albumin, PMFA (protein migrating faster than albumin) and lysozyme was accomplished by gel permeation chromatography in less than 30 min using a TSK-type SW3000 column equilibrated with ammonium acetate buffer (pH 4.1) with a high reproducibility. When gel permeation chromatography was used as a completely automated diagnostic method, only minute volumes (1.0 microliter) of tear samples were necessary for the quantitative analysis of proteins. The other three methods proved to be more suitable for the preparation of individual tear proteins but were less suitable for their quantitation.
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PMID:Analysis of human tear proteins by different high-performance liquid chromatographic techniques. 232 62

Proteins and mucosubstance of the saline extract of human ocular mucus were studied by immunological analysis. A minor study was made with human tears for comparison. Immunoelectrophoresis of proteins from these two sources consistently revealed similar characteristic gel patterns. Proteins were found as the major constituents of both samples. However, more mucosubstance was present in the saline extract of human ocular mucus than in tears. Seventeen proteins were identified in the mucus extract. Albumin, IgA, and lactoferrin appeared to be the three major proteins, while lysozyme, lactoferrin, tear prealbumin, and ocular mucoisolate were tear and ocular mucus specific. Although saline soluble mucoisolate is complex in structure, it seemed to resist electrical dissociation, producing only one major precipitation line along with a line of IgA during immunoelectrophoresis. The ocular mucoisolate accounted for about 12% of the saline extractable proteins of human ocular mucus.
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PMID:Immunological study of proteins and mucosubstance in saline soluble human ocular mucus. 310 26

Tear fluid is a mixed solution containing many kinds of proteins, and two predominant fractions have been determined by electrophoretic studies. One is anodal specific tear prealbumin (STP) and the other is cathodal lysozyme. This study is the first to demonstrate the localization of STP in the ocular adnexa by the immunofluorescence method. STP was found in the acinar cells of both the main and the accessory lacrimal glands. The cells of the interlobular ducts showed no or only weak staining of STP. No specific staining of STP was found in the conjunctiva, cornea or Meibomian gland. STP as well as lysozyme are thought to be secreted from the main and the accessory lacrimal glands.
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PMID:Studies of human tear proteins. 3. Distribution of specific tear prealbumin in lacrimal glands and other ocular adnexa. 653 Aug 34

The protein composition of normal and pathological tears was studied by polyacrylamide-gel (disc) electrophoresis. Polyacrylamide-gel electrophoresis was shown to detect at least 14 fractions in 2-10 microliters of native tears. A comparison was made between the protein composition of normal tears and serum. The most characteristic bands in the tear-protein pattern were identified by parallel electrophoresis of tears, serum, human milk and purified egg-white lysozyme. The identified fractions were specific tear prealbumin, serum albumin, transferrin, lactoferrin and lysozyme. An unidentified major tear-protein component was also described. The tear-protein pattern was divided into six zones: (1) prealbumin zone; (2) post-albumin zone; (3) post-transferrin zone; (4) macroglobulin zone; (5) basic globulin zone; (6) prelactoferrin zone. A significant rise in the level of serum albumin and transferrin was demonstrated in tears from cases of acute catarrhal conjunctivitis. The optimal circumstances were discussed under which major and minor tear components and basic and acidic tear proteins can be determined simultaneously. Polyacrylamide-gel electrophoresis is recommended as a useful method to study the various diseases of the anterior segment of the eye.
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PMID:A polyacrylamide-gel electrophoretic study of human tear proteins. 714 Dec 35

Tears were collected from 10 normal subjects by two methods, 1) micropipetting after stimulation with an onion slice, and 2) Schirmer 1 test using a filter paper strip. The tears in the 5 x 5 mm part of the filter paper placed within the conjunctival sac were extracted with a 0.9% NaCl solution. The tear samples so obtained were analyzed by crossed immunoelectrophoresis. Nineteen proteins were identified by the use of monospecific antisera. Ten tear-specific proteins including the specific tear prealbumin of Bonavida et al., lactoferrin and lysozyme were identified by the intermediate gel method. Some differences were found in the pattern of the tear-specific proteins between the tears collected by the two methods, but the pattern was basically similar. Some individual differences were also found. The levels of serum proteins including albumin and IgG varied considerably, but it was thought to be due to dilution by reflex lacrimation during tear sampling. On the other hand, the pattern of the tear-specific proteins was fairly constant. The filter paper method allowed tear protein analysis, even in patients with 0 mm wetting by the Schirmer 1 test. A study of the length-volume relationship of the filter paper wetting showed that the tears contained in the 5 x 5 mm portion of the filter paper were about 1.8 microliters. The filter paper method was thought to offer a reliable clinical tool for the study of the tear proteins in various pathological conditions of the lacrimal secretion.
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PMID:Studies of human tear proteins--1. Analysis of tears from normal subjects by crossed immunoelectrophoresis. 715 27

The purpose of this study was to investigate lacrymal component accumulation on a soft contact lens (SCL) surface after various periods of continuous wear, using the recently developed atomic force microscopy (AFM). AFM allowed high resolution images of unworn and worn SCL, and presented two main advantages. 1. The SCL are analysed under nearly physiological conditions without being dried or destroyed. So the same SCL was analysed at various times during a long wearing period. To identify the deposited tear proteins, a qualitative analysis of solubilized deposit by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) on 4-15% gradient minigels was performed as well. We present typical images which emphasize the importance of the coating by lacrymal components. AFM analysis of worn SCL showed the deposition on the surface of a uniform lacrymal component coating (named deposit type I) with a progressive accumulation of numerous discrete granules (named deposit type II). SDS-PAGE of extracted deposits revealed the main tear proteins as: IgA, lactoferrin, tear lipocalin and lysozyme and the unknown protein of molecular weight 30,000. There is no clear difference in the protein patterns of the two types of deposits. Furthermore, a particular mode of use of AFM is described to illustrate the potential of this technique as a local tool for measuring protein coating thickness. Thus, for analysis of protein deposits on SCL surfaces, SDS-PAGE on minigels and AFM were easy and rapid to perform. When associated, these two techniques could find use in a wide range of worn SCL evaluation and most generally in biocompatibility evaluation studies.
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PMID:Characterization of lacrymal component accumulation on worn soft contact lens surfaces by atomic force microscopy. 771 89

The eyes are protected by the mechanical action of blinking and the washing action of tears; besides maintaining comfort and serving as the optical surface, the tear film forms the first line of defence. This role is mainly due to specific action of secretory immunoglobulins and continuous presence of unspecific proteins such as lysozyme, lactoferrin and tear lipocalin.
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PMID:[Defense proteins in the corneo-conjunctival epithelium]. 934 7

The interaction of human tear lipocalin with lysozyme and lactoferrin was studied by electron paramagnetic resonance (EPR) spectroscopy. TL mutants I98C and F99C were spin labeled with MTSL and its derivative. The spectra demonstrated that at sites C98 and C99 the mobility of the nitroxides was reduced in the presence of lysozyme, lactoferrin, but not albumin. The reduced mobility was manifested as a reduction in side chain motion and backbone fluctuations. The overall correlation time of tear lipocalin, measured by MTSL derivative-labeled F99C, was prolonged in the presence of lysozyme and lactoferrin indicating that the interaction involves direct contact. The effect was mitigated at high salt concentration suggesting an electrostatic interaction of the molecules. The reduction in side chain mobility at C98 and C99 of tear lipocalin was observed in tears. Taken together, the data indicate that tear lipocalin interacts with both lysozyme and lactoferrin and suggest that they may function in concert with one another.
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PMID:Interaction of tear lipocalin with lysozyme and lactoferrin. 1055 65

New cysteine protease inhibitors in human tears and milk and their medical significance are reviewed in this paper. As protective components against bacterial infection in the eyes, we detected four kinds of anti-bacterial proteins in normal human tears including lysozyme and three kinds of cysteine protease inhibitors. Using our reverse zymography of normal tears, three kinds of cysteine protease inhibitors were found to be 78kDa, 20kDa and 15kDa and were determined to be lactoferrin, Von Ebner's Gland (VEG) protein and cystatin S, respectively. All of them belong to the cystatin super family and VEG protein and cystatin S are well known cysteine protease inhibitors. The C-terminus area 17mer peptide, Y679-K695, of lactoferrin showed strong homology with a common active domain of the cystatin family and the synthesized peptide showed inhibition of cysteine proteases. Not only were disease-specific changes found in these inhibitor profiles, but also disease-specific new inhibitors in patients tears with certain autoimmune diseases. A 35kDa inhibitor, which was detected specifically in tears with Behcet's disease, an typical autoimmune disease, was determined to be a lacrimal acidic proline-rich protein based on the N-terminus sequence analysis. A 65kDa inhibitor of tears with Harada's autoimmune disease was determined to be an Ig heavy chain V-III region. In addition, lactoferrin content in Harada's disease was very low. We found two cathepsin inhibitors in bovine milk using reverse zymography, namely lactoferrin and beta-casein. The L133-Q151, in the human beta-casein molecule is the active inhibitory domain. They may play an important role in antiseptic and anti-infectious functions.
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PMID:Medical significance of cysteine protease inhibitors in mammalian secretory fluids. 1367 84


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