Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Protein antigenic determinants have been classified as continuous or discontinuous. The continuous determinants are composed of residues which are local in the polypeptide sequence, while discontinuous determinants consist of residues from different parts of the sequence, brought together by the folding of the protein to its native structure. Searches made for protein determinants using peptide fragments which compete with protein-antibody complex formation, or peptides that can be used to raise antibodies which crossreact with the native protein, are limited to the simulation of continuous determinants. However, recent experiments suggest that most determinants are discontinuous. We now show, by consideration of protein surfaces, that if the recognition zone between a protein and antibody has the same dimensions as those found for the lysozyme-antibody complex, none of the protein's surface will be 'continuous'. We suggest that all determinants are discontinuous to some extent, and that crossreacting peptides mimic only the 'primary' interaction site. In addition, we show that the parts of a protein's surface which are most continuous fall predominantly in the loops and/or protruding regions. This explains why quantities such as hydrophilicity, accessibility, mobility and protrusion can be used to predict which parts of a polypeptide provide the 'best' antigenic peptides.
...
PMID:Continuous and discontinuous protein antigenic determinants. 242 53

The cellular sediments of 42 malignant and 16 benign effusions (58 cases) were studied using the immunoperoxidase technique. Serial sections of formalin-fixed, paraffin-embedded residual sediments of effusions, sent for routine cytologic examination, were studied by commercially available polyclonal antisera against lysozyme, alpha 1-anti-trypsin, alpha 1-anti-chymotrypsin, tissue polypeptide antigen (TPA), a wide-spectrum anti-keratin, carcinoembryonic antigen (CEA) and, in single cases, thyroglobulin and prostate-specific antigen. A final definite diagnosis from histologic study of biopsy or autopsy specimens was known in all cases. All carcinomas, the mesotheliomas and the reactive mesothelial cells showed a positive reaction for TPA and, partly, the wide-spectrum keratin. Lysozyme could be demonstrated in the cells of the one proven malignant fibrous histiocytoma; all malignant epithelial cells were negative. Alpha 1-anti-chymotrypsin and alpha 1-anti-trypsin showed similar reactions: they were often positive in carcinoma cells of the breast, the bronchial system and the pancreas, in contrast to a mostly negative reaction in carcinomas of the stomach and ovary. CEA showed considerable differences; it was always negative in benign and malignant mesothelial proliferations but mostly positive in carcinomas of the stomach, pancreas and bronchial system. It was only positive in less than 20% of the carcinomas of the breast and always negative in the proven malignant effusions of primary carcinomas of the ovary and prostate. Studying a combination of several tumor markers is possible in serial paraffin-embedded sections and may be a valuable criterion in the cytologic diagnosis of effusions.
...
PMID:Immunohistochemical study of lysozyme, alpha 1-anti-chymotrypsin, tissue polypeptide antigen, keratin and carcinoembryonic antigen in effusion sediments. 243 1

Sections of primary lung carcinomas, lung metastases, mesotheliomas, and lung metastases of some rare mesenchymal tumors were incubated with different cytokeratin (CK), vimentin, desmin, and tissue polypeptide antigen (TPA) antibodies and with antibodies reactive with different hormones (ACTH, PTH, alpha-HCG, Calcitonin CT), CEA, carcinoma-associated antigen (CA1), secretory component (SC), neuron-specific enolase (NSE), alpha-1-antitrypsin (alpha-1-AT), lysozyme (lyso), and S-100 protein (S 100). CK antibodies derived from a 49 kD (reactive with simple epithelia [SE]) and a 67 kD CK polypeptide fraction (reaction with complex epithelia [CE] were useful differentiation markers for the four major groups of lung carcinomas. In one half of small cell carcinomas a positive reaction with NSE antibodies was found. S 100 and SC were good markers for papillary and bronchioloalveolar adenocarcinomas, whereas CEA was less important because of its reactivity with different types of lung carcinomas. To discern clear cell carcinomas of lung and renal origin a positive reaction with vimentin antibodies (some renal but not lung types) and with CA1 (no renal but all lung types) seemed to be useful. All hormone antibodies were of no importance as markers for difficult differential diagnosis, because positive reactivities were found in cases from every major carcinoma group. In addition, a Ca2+-activated adenosine triphosphatase (ATPase) was found in mesotheliomas but not in papillary adenocarcinomas.
...
PMID:Immunohistochemical and histochemical markers of primary lung cancer, lung metastases, and pleural mesotheliomas. 243 80

We have reviewed here the three-dimensional structure of an antigen-Fab complex as determined by X-ray crystallographic studies. The antigen is hen egg-white lysozyme (HEL), a protein whose three-dimensional structure and antigenic properties are well known. The Fab was prepared from a murine monoclonal anti-HEL antibody, IgGl,kappa, obtained by cell-hybridization techniques. The equilibrium association constant for the complex is 4.5 X 10(7) mol-1. The complex was crystallized and its three-dimensional structure was determined at 6-A and 2.8-A resolution. A three-dimensional model of the structure was built based on electron-density maps and the amino-acid sequence [determined from the nucleotide sequence of cDNA clones (M. Verhoeyen, C. Berek, J.M. Jarvis, G. Winter, in preparation)]. The three-dimensional structure of the complex shows that 17 antibody residues make close contacts (less than or equal to 4 A) with 16 antigen residues. Fifteen of the contacting antibody residues belong to the six complementarity-determining regions of the light chain (6 residues) and of the heavy chain (9 residues). The remaining two are located in regions of constant or nearly constant sequence ["framework" regions]. The 16 contacting lysozyme residues form a discontinuous, topographical determinant, since they are widely separated in the linear amino-acid sequence but are brought to relative spatial proximity by the three-dimensional folding of the polypeptide chain. The contacting surfaces are relatively flat, with protruding side chains of antigen and antibody penetrating each other over an area with maximum dimensions of 30 X 20 A. As in several other systems of protein-protein interactions, the contacts are chemically characterized as van der Waals interactions and hydrogen bonds. Detailed analysis of the interactions reveals that the antibody's recognition of the antigen is finely specific and is affected by antigenic variation (as observed in lysozymes from other avian species). The quaternary structure of the complexed Fab is elongated, with the axes of the variable (VH + VL) and constant (CH1 + CL) domains making an angle close to 180 degrees. Comparison of the three-dimensional structure of the complexed lysozyme with that of native lysozyme showed no significant conformational change at the current resolution (2.8 A). Comparison of the Fab moiety of the complex with other Fabs of known three-dimensional structure suggested that upon complexing no conformational change takes place in the tertiary structure of Fab either.(ABSTRACT TRUNCATED AT 400 WORDS)
...
PMID:The structural basis of antigen-antibody recognition. 243 94

The binding pattern of antibodies against different cytokeratin (CK) polypeptides, tissue polypeptide antigen (TPA), carcinoembryonic antigen (CEA), lactoferrin (Lf), lysozyme (Ly) and secretory component (SC) in palatal glands (PSG) of long-term denture wearing patients has been studied to investigate immunohistochemically the localization of these marker proteins in normal PSG and in denture-induced sialadenitis of PSG. The study included palatal gland biopsies from 28 patients (15 f, 13 m; mean age 59 years), 17 of them with normal PSGs, 8 with focal obstructive sialadenitis, and 3 with diffuse sialadenitis. Presence of CK and TPA was found in all intra- and extraglandular salivary ducts, in the basophilic portions of acini, in some mucous acini, and in all atrophic acini. Increased expression of CEA and Lf was observed in inflammed areas of PSG which, on the other site, were devoid of Ly and SC. In the mucous acini of healthy PSG considerable basal Ly immunoreactivity was seen. SC was localized in almost all ductal cells and in some acinar cells. Appearance of Lf in the ductal cells of PSG indicates an early sign of palatal sialadenitis. Some distinctions in the expression pattern of the marker proteins between the mucous acini of major salivary glands and PSG point to differences in the functional activities of either group of salivary glands.
...
PMID:Immunohistochemical study of palatal salivary glands of denture wearing patients. 246 20

31P-NMR and X-ray diffraction techniques are used to study the comparative ability of myelin basic protein (MBP) vs. other basic proteins to convert hexagonal (HII) phases to stable lamellar (L alpha) structures. Pure dioleoylphosphatidylethanolamine (DOPE) at pH 9 and 7, and mixtures of DOPE/phosphatidylserine (PS) (95:5 and 80:20% w/w) at pH 7 were employed for this investigation. The polymorphic behavior of the lipid suspensions was evaluated in the presence and absence of several basic proteins (MBP, calf thymus histone, lysozyme, melittin) and the cationic polypeptide, polylysine (PL). Each of the proteins and PL was capable of binding the pure DOPE HII phase at pH 9 but with varying morphological consequences, i.e., lamellar stabilization (MBP, histone, PL), formation of new protein-DOPE HII phases (lysozyme) or lipid disordering/vesiculation (melittin). Reduction to pH 7 resulted in the dissociation of protein from DOPE - with the exception of melittin - and the reformation of a pure lipid HII phase. Additions of PS to DOPE at pH 7 facilitated protein binding, but among the proteins examined, only MBP was capable of converting the lipid suspension into a stable multilamellar form. Differences in the lipid morphology produced by each protein are discussed in terms of protein physicochemical characteristics. In addition, a possible relationship between MBP-lipid interactions and the stability of myelin sheath lipid multilayers is inferred from the significant bilayer-stabilizing capacity of MBP.
...
PMID:Bilayer-stabilizing properties of myelin basic protein in dioleoylphosphatidylethanolamine systems. 247 28

Immunohistochemical demonstration of cytokeratin (CK), tissue polypeptide antigen (TPA), carcinoembryonic antigen (CEA), lactoferrin (Lf), lysozyme (Ly) and secretory component (SC) was performed in major salivary glands (MaSG), labial and palatal salivary glands (LSG, PSG). CK and TPA were demonstrated in ductal cells of all SGs. In addition, binding of anti-CK (Mw-56 Kd) antibody (AB) KL I was seen in all serious acini of MaSG, basophilic acini and demilunes of LSG and in some mucous acini of PSG. Binding of anti-CK (Mw 44-54 Kd) AB-PKK I, another polyclonal anti-CK (Mw 55-67 Kd) AB-PCK and anti-TPA AB was demonstrated in all basophilic acini of LSG, basophilic portions of mucous acini in PSG and not in acini of MaSG. Significant differences were observed in the expression of CEA, Ly, Lf and SC between acini of MaSG and MiSG which probably reflects different functions of these glands.
...
PMID:Localization of epithelial markers and defence proteins in minor and major salivary glands. 247 85

Primary carcinoid tumours of the middle ear are extremely rare, only nine cases having been reported. However, their true incidence is probably greater, since they are very difficult or impossible to distinguish from adenomas and adenocarcinomas with conventional histological stains. We describe the clinical, histological, immunohistochemical and ultrastructural findings in a carcinoid tumour of the middle ear in a 50-year-old woman. Immunohistochemical studies on non-neoplastic middle ear mucosa undertaken to investigate the histogenesis of such tumours are also reported. Histologically, the tumour consisted of both solid areas and areas of tubular structures containing intraluminal mucus. All the tumour cells reacted with the anti-keratin antibody KL 1; some were argyrophil and reacted with antibodies against neuron-specific enolase, chromogranin A, Leu-7, serotonin, pancreatic polypeptide, glucagon and lysozyme. Electron microscopy revealed dense core granules in the tumour cells. Endocrine cells could not be detected in non-neoplastic middle ear mucosa. Pancreatic-polypeptide-like immunoreactivity was demonstrated immunohistochemically in all three other published cases of carcinoid tumour of the middle ear investigated for this peptide, and glucagon-like immunoreactivity was also exhibited by one of these. Since carcinoid tumours of the middle ear often, as in this case, exhibit some degree of glandular differentiation, immunohistochemical or electron-microscopic investigation to detect neuroendocrine differentiation is of particular importance in adenomatous middle ear neoplasms.
...
PMID:Carcinoid tumour of the middle ear. A morphological and immunohistochemical study with comments on histogenesis and differential diagnosis. 248 Dec 99

Heat capacity, intrinsic viscosity and ellipticity of a number of globular proteins (pancreatic ribonuclease A, staphylococcal nuclease, hen egg-white lysozyme, myoglobin and cytochrome c) and a fibrillar protein (collagen) in various states (native, denatured, with and without disulfide crosslinks or a heme) have been studied experimentally over a broad range of temperatures. It is shown that the partial heat capacity of denatured protein significantly exceeds the heat capacity of native protein, especially in the case of globular proteins, and is close to the value calculated for an extended polypeptide chain from the known heat capacities of individual amino acid residues. The significant residual structure that appears at room temperature in the denatured states of some globular proteins (e.g. myoglobin and lysozyme) at neutral pH results in a slight decrease of the heat capacity, probably due to partial screening of the protein non-polar groups from water. The heat capacity of the unfolded state increases asymptotically, approaching a constant value at about 100 degrees C. The temperature dependence of the heat capacity of the native state, which can be determined over a much shorter range of temperature than that of the denatured state and, correspondingly, is less certain, appears to be linear up to 80 degrees C. Therefore, the denaturational heat capacity increment seems to be temperature-dependent and is likely to decrease to zero at about 140 degrees C.
...
PMID:Heat capacity and conformation of proteins in the denatured state. 253 36

The "vapor-phase" hydrazinolysis method was devised for the microdetermination of the carboxyl-terminal residue of a protein. With this method, a polypeptide sample is degraded with vaporized hydrazine. The optimum conditions for hen egg-white lysozyme were established to be 2 to 4 h at 90 or 100 degrees C, the recovery of the carboxyl-terminal leucine being about 70%. With this vapor-phase method, side reactions are reduced and the time of hydrazinolysis is shortened. The limit of quantitation for the carboxyl-terminus of a protein is about 50 pmol, as judged so far with hen egg-white lysozyme. The carboxyl-termini of several proteins were determined using this novel procedure.
...
PMID:Vapor-phase hydrazinolysis for microdetermination of carboxyl-terminal amino acids of proteins. 260 8


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---