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)

Breast secretions can be classified into two types according to their major protein components. Type I fluids contain Zn-alpha 2-glycoprotein, apolipoprotein D, and gross cystic disease fluid protein-15, while Type II fluids are characterized by the presence of lactoferrin, lysozyme, and alpha-lactalbumin. In this study, the polypeptide composition of breast secretions from 719 nonlactating women was evaluated by using polyacrylamide gel electrophoresis. The required amount for the analysis (1 microliter) was obtained from 50% of control women and from 75% of women with mammary disease. There were more secretors in premenopausal than in postmenopausal women, as well as in parous than in nulliparous women. Evaluation of factors affecting protein composition of breast secretions revealed that Type II fluids were found in the majority of women who had given birth in the last four years and in a high proportion of oral contraceptive users. After excluding both of these groups, Type II fluids were detected in 47% of patients with breast cancer, but only in 8% of control women and in 16% of women with benign breast diseases. Taken together, these results suggest that protein analysis of breast secretions could be an useful tool for the study of breast pathologies.
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PMID:Factors affecting protein composition of breast secretions from nonlactating women. 146 65

The protein composition of breast secretions from 99 premenopausal women with benign or malignant breast diseases and from 70 control women without breast pathologies has been studied by using polyacrylamide gel electrophoresis. These fluids have been classified into two types according to their major polypeptide components. Type I fluids are defined by three major distinctive bands at Mr 44,000, 24,000, and 17,000, while those designated Type II present distinctive bands at Mr 80,000, 15,000, and 14,000. Amino acid sequencing and immunoblotting analysis demonstrated that proteins in Type I secretions correspond to Zn-alpha 2-glycoprotein, apolipoprotein D, and gross cystic disease fluid protein-15, while those from Type II fluids have been identified as lactoferrin, lysozyme, and alpha-lactalbumin. Most women (93%) without breast pathology and most patients (88%) with benign diseases had secretions with a Type I polypeptide pattern. By contrast, a large percentage (57%) of secretions from women with breast carcinoma presented a Type II protein pattern. Further studies with a large number of women will be useful for corroborating the potential clinical interest of breast fluid protein analysis.
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PMID:Identification of the major protein components in breast secretions from women with benign and malignant breast diseases. 172 90

Sweat samples were collected in a sauna from 74 healthy volunteers (72 men and 2 women) and concentrated. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) of the individual samples revealed, in general, five main proteins and four PAS positive components. In pooled sweat, a method of SDS-PAGE followed by immunoblotting with specific antisera or antibodies against 24 human serum components was applied, and three out of the five main proteins showed the same molecular weights and antigenicities corresponding to serum albumin (67,000 Da), Zn-alpha 2-glycoprotein (42,000 Da) and lysozyme (14,000 Da). Moreover, orosomucoid, transferrin, IgG and IgA were demonstrated in the pooled sweat. Although alpha 1-antitrypsin was probably in the pooled sweat, other serum components could not be detected. On the pooled and individual sweat samples, anti-carcinoembryonic antigen (CEA) formed three bands at 42,000, 19,000 and 18,000 Da, but the antibody did not react with normal serum. It might be considered from these molecular weights that those sweat components are CEA-related antigens.
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PMID:Sweat protein components tested by SDS-polyacrylamide gel electrophoresis followed by immunoblotting. 239 53

Elimination of low molecular weight proteins during sequential ultrafiltration/dialysis was studied in 29 uremic patients. Beta-2-microglobulin, retinol binding protein, free light chains lambda and kappa, Zn-alpha-2-glycoprotein, hemopexin, prealbumin, hemoglobin, albumin, acid alpha-1-glycoprotein, haptoglobin, alpha-1-antichymotrypsin, ribonuclease, lysozyme, amylase, non-specific esterase, and proteolytic activity were detected in all ultrafiltrates tested. The level of total protein and ribonuclease was determined in 36 crude ultrafiltrates from 23 patients. Concentrated ultrafiltrates were used to quantitate retinol binding protein, prealbumin, albumin, lysozyme, and amylase. Other proteins identified in the ultrafiltrates are present in trace amounts. The question was discussed whether ++inextensive but systematic loss of proteins during hemofiltration in chronic RDT might be the cause of patient homeostasis disturbances.
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PMID:Detection of plasma proteins during sequential ultrafiltration/dialysis. 406 85

The potential relationship between serum PRL levels and protein composition of breast secretions was evaluated in 54 premenopausal nonlactating women during the luteal phase of their menstrual cycle. Women were classified into four groups according to the presence or absence of breast pathology and to the protein pattern of their breast secretions. Type I mammary fluids contain Zn-alpha 2-glycoprotein, apolipoprotein D, and gross cystic disease fluid protein-15, whereas Type II fluids are characterized by the presence of some milk proteins such as lactoferrin, lysozyme, and alpha-lactalbumin. Basal serum levels of PRL, as well as of progesterone, LH, FSH, TSH, T3, and T4 were within normal range, and no significant differences were found between the different groups of women under study. However, after a TRH stimulation test, the maximum PRL response was significantly higher (P < 0.02) in normal women with Type II secretions than in those with Type I (64 +/- 6.8 micrograms/L vs. 43.7 +/- 3.9 micrograms/L). Similarly, when PRL concentrations in patients with benign breast disease were considered, those with breast fluids containing milk proteins had a rise in PRL secretion after TRH stimulation significantly higher (P < 0.05) than those with fluids lacking these proteins (77.1 +/- 6.2 vs. 58.8 +/- 5.1 micrograms/L). These results indicate that the occurrence of milk proteins in breast secretions from nonlactating women is associated with an increase in serum PRL concentrations after TRH stimulation, and opens the possibility of using breast fluid protein analysis as a simple and noninvasive procedure for studies on the putative role of PRL in the development of benign and malignant breast diseases.
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PMID:Relationship between serum prolactin levels and protein composition of breast secretions in nonlactating women. 804 72

Saliva plays many biological roles, from lubrication and digestion to regulating bacterial and leukocyte adhesion. To understand the functions of individual components and families of molecules, it is important to identify as many salivary proteins as possible. Toward this goal, we used a proteomic approach as the first step in a global analysis of this important body fluid. We collected parotid saliva as the ductal secretion from three human donors and separated the protein components by two-dimensional SDS-polyacrylamide gel electrophoresis (2D SDS-PAGE). Proteins in gel spots were identified by peptide mass fingerprinting, and the results were confirmed by tandem mass spectrometry of selected peptides. Complementing this approach we used ultrafiltration to prepare a low-molecular-weight fraction of parotid saliva, which was analyzed directly or after reversed phase high-performance liquid chromatography separation by using mass spectrometric approaches. MS analyses of 2D SDS-PAGE spots revealed known components of saliva, including cystatins, histatins, lysozyme, and isoforms and/or fragments of alpha-amylase, albumin, and proline-rich proteins. We also discovered novel proteins, such as several isoforms of Zn-alpha-2-glycoprotein and secretory actin-binding protein. MS analyses of the ultrafiltrate showed that the low-molecular-weight fraction of parotid saliva was peptide-rich, with novel fragments of proline-rich proteins and histatins in abundance. Experiments using Candida albicans as the test organism showed that at least one of the novel peptides had antifungal activity. Our results show that saliva is a rich source of proteins and peptides that are potential diagnostic and therapeutic targets.
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PMID:Toward defining the human parotid gland salivary proteome and peptidome: identification and characterization using 2D SDS-PAGE, ultrafiltration, HPLC, and mass spectrometry. 1572 31