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)

The protein/biomaterial interactions of three biomaterials used in hard tissue surgery were studied in vitro. A dynamic flow system and two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) were used to investigate the adsorption of proteins from diluted human plasma on hydroxyapatite, alumina and zirconia, with regard to total protein binding capacity, relative binding capacity for specific proteins and flow-through and desorption patterns. The ceramics were characterized regarding physicochemical properties; namely, chemical composition by elementary analyses and specific surface, pore volume and pore size distribution using the BET-method and Hg-porosimetry. The materials were found to adsorb a surprisingly low amount of plasma proteins, leaving more than 70% of the surface free. The cellular response will therefore be highly affected by the physico-chemical properties of the material, in contrast to a surface fully covered with proteins. Regarding the adsorption of proteins, most proteins exhibited similar flow-through patterns on the three adsorbents. The exceptions with different flow-through patterns were apolipoprotein D (Apo D), apolipoprotein J (Apo J), complement factor C1s (C1s), complement factor C3 (C3), ceruloplasmin, fibrinogen, alpha1 B glycoprotein and alpha2 HS glycoprotein and serum retinal-binding protein (SRBP). The role of these proteins on acceptance or rejection of implants has to be investigated.
 ...
PMID:Plasma protein adsorption pattern on characterized ceramic biomaterials. 1179 28

Glycosylation is the most abundant and complex protein modification, and can have a profound structural and functional effect on the conjugate. The oligosaccharide fraction is recognized to be involved in multiple biological processes, and to affect proteins physical properties, and has consequentially been labeled a critical quality attribute of biopharmaceuticals. Additionally, due to recent advances in analytical methods and analysis software, glycosylation is targeted in the search for disease biomarkers for early diagnosis and patient stratification. Biofluids such as saliva, serum or plasma are of great use in this regard, as they are easily accessible and can provide relevant glycosylation information. Thus, as the assessment of protein glycosylation is becoming a major element in clinical and biopharmaceutical research, this review aims to convey the current state of knowledge on the N-glycosylation of the major plasma glycoproteins alpha-1-acid glycoprotein, alpha-1-antitrypsin, alpha-1B-glycoprotein, alpha-2-HS-glycoprotein, alpha-2-macroglobulin, antithrombin-III, apolipoprotein B-100, apolipoprotein D, apolipoprotein F, beta-2-glycoprotein 1, ceruloplasmin, fibrinogen, immunoglobulin (Ig) A, IgG, IgM, haptoglobin, hemopexin, histidine-rich glycoprotein, kininogen-1, serotransferrin, vitronectin, and zinc-alpha-2-glycoprotein. In addition, the less abundant immunoglobulins D and E are included because of their major relevance in immunology and biopharmaceutical research. Where available, the glycosylation is described in a site-specific manner. In the discussion, we put the glycosylation of individual proteins into perspective and speculate how the individual proteins may contribute to a total plasma N-glycosylation profile determined at the released glycan level.
 ...
PMID:Human plasma protein N-glycosylation. 2655 91