Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We determined serum levels of alpha 1-antitrypsin, alpha 1-acid glycoprotein, ceruloplasmin, haptoglobin, alpha 2-HS glycoprotein, C3 and fibronectin in 22 patients with acute pneumonia, 10 patients with mycoplasma pneumonia and 8 patients with exacerbation of chronic bronchitis at both acute and convalescent phases to clarify whether levels of these proteins change with inflammation. Serum levels of alpha 1-antitrypsin, alpha 1-acid glycoprotein, ceruloplasmin, haptoglobin and C3 in the patients in the acute phase were significantly higher than that in the patients in the convalescent phase. The serum level of fibronectin in the patients in the acute phase was significantly lower than that in the patients in convalescent phase. The serum level of alpha 2HS glycoprotein remained unchanged.
 ...
PMID:[Changes in various serum protein levels between acute and convalescent phases in patients with respiratory infections]. 169 92

A microattachment assay for quantitating adherence of radiolabelled Mycoplasma pneumoniae to human WiDr cell culture monolayers is described. Preincubating the WiDr cell monolayers with a protein-rich extract of M. pneumoniae inhibited the subsequent attachment of radiolabelled organisms. Competitive attachment inhibition provided a quantitative procedure to determine M. pneumoniae-binding components in the extract. The microattachment assays also measured attachment inhibition by the sialoglycoconjugates ceruloplasmin, orosomucoid and gangliosides, indicating that these reagents may be structural analogues of the mammalian cell receptor. Attachment of virulent M. pneumoniae strains to glutaraldehyde-treated monolayers was reduced approximately 60% and showed a different temperature dependence compared with untreated cells. These results suggest that maximal attachment of virulent M. pneumoniae may require two or more different receptors and binding components.
 ...
PMID:Competitive inhibition and attachment assays in cell cultures to detect pathogenic binding components of mycoplasmas: a review. 642 26

Attachment of Mycoplasma pneumoniae to human WiDr cell culture monolayers was examined by using radiolabeled M. pneumoniae. The amount of attachment was proportional to the density of the WiDr cells and to the concentration of M. pneumoniae in the assay. Saturation of the monolayers was achieved with 40 micrograms of virulent strain M129 per assay, whereas binding of avirulent strain B176 was 70% less than that of strain M129. A competitive attachment inhibition assay was used to measure specific binding component activity. Attachment was inhibited when WiDr cells were pretreated with unlabeled virulent strain M129, whereas avirulent noncytadsorbing strain B176 did not inhibit attachment as well as the virulent strain. A protein-rich extract prepared from virulent, cytadsorbing strains of M. pneumoniae also inhibited attachment. The amount of inhibition was dependent on the amount of extract used, and units for binding component activity in the extract were calculated from the competitive attachment inhibition assays. The competitive attachment inhibition assay was also used to investigate the nature of the receptor site on the WiDr cells. Attachment was inhibited when the radiolabeled M. pneumoniae suspensions were pretreated with human sialoglycoproteins, such as orosomucoid and ceruloplasmin, and bovine gangliosides. These findings support the present concept that the mammalian receptor site for M. pneumoniae is a sialic acid-containing glycoprotein.
 ...
PMID:Mycoplasma pneumoniae attachment: competitive inhibition by mycoplasmal binding component and by sialic acid-containing glycoconjugates. 681 97