apoprotein

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Related to Apoproteins: lipoprotein lipase

apoprotein

 [ap″o-pro´tēn]
the protein portion of a molecule or complex consisting of a protein molecule joined to a nonprotein protein molecule or molecules (such as a lipoprotein).

ap·o·pro·tein

(ap'ō-prō'tēn),
A polypeptide chain (protein) that has not yet formed a complex with the prosthetic group required to form the active holoprotein.

apoprotein

/apo·pro·tein/ (ap″o-pro´tēn) the protein moiety of a molecule or complex, as of a lipoprotein.

apoprotein

[ap′ōprō′tēn]
a polypeptide chain not yet complexed to its specific prosthetic group.

apoprotein

The protein part of a biomolecular complex without its ligand or prothetic group (e.g., ferritin without ferric hydroxide = apoferritin).

ap·o·pro·tein

(ap'ō-prō'tēn)
A polypeptide chain (protein) not yet complexed with the prosthetic group that is necessary to form the active holoprotein.

apoprotein

the protein moiety of a molecule or complex, as of a lipoprotein.
References in periodicals archive ?
Second, although it is now recognized that the hydrophobic apoproteins SP-B and SP-C are required to create the lung lining film and for it to vary surface tension, (2) in most neonatal patients there is enough "extra" endogenous apoproteins SP-B/C to incorporate any exogenous phospholipids instilled into the lungs to significantly improve the function of the lining film.
Lipids, lipoproteins, and apoproteins in serum during infection.
All lipoproteins contain cholesterol, phospholipids, triglycerides, and apoproteins to maintain structural integrity.
The sticking point is that when carrier molecules, called apoproteins, combine with non-water-soluble cholesterol (meaning it doesn't dissolve in blood), they form lipoproteins.
Among the classic risk factors for coronary artery disease are elevated blood levels of cholesterol (in low-density and very-low-density lipoproteins), triglycerides, certain apoproteins), triglycerides, certain apoproteins and uric acid.
Essentially all circulating apoB is associated with lipoproteins, and unlike most other apoproteins, apoB cannot exchange freely among lipoprotein particles (2, 3).
LPL also contributes to the exchange of lipids and apoproteins between different lipoprotein classes, thus affecting size and composition not only of TG-rich lipoproteins but also of low and high density lipoproteins (LDL and HDL) (Eisenberg, 1984; Goldberg, 1996).
2] results from the transfer of phospholipids, free cholesterol, and apoproteins, released from the lipolyzed VLDLs, to the HDL particle (Eisenberg 1984).
Mouse monoclonal antibodies directed against the following components were used: HMB-45, which recognizes gp100[23] and serves as a marker for epithelioid LAM cells[11] (Dako; dilution, 1:200); PCNA (Dako; dilution, 1:100), which is localized in the smaller, spindle-shaped LAM cells[8,13]; PE-10 (Dako; dilution, 1:200), which reacts with the surfactant apoprotein A found in type II pneumocytes[24]; and TTF-1 (Neomarkers, Inc, Union City, Calif; dilution, 1:75), which identifies a nuclear transcription factor for surfactant apoproteins A and B and is present in the nuclei of type II pneumocytes.
Thus, apoproteins show less S-thiolation than expected from their free -SH content, and S-thiolation is probably limited by the accessibility of the same -SH residues.