Maro Publications

Albumin

From 06/02/2014 through 9/2/2013

Notes

Patent Abstracts

Patent Titles

 

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Patent Titles

1/28/2014

2. 8,635,752 
Devices for abluminally coating medical devices 

10/8/2013

1. 8,551,948 
Albumin fibers and fabrics and methods of generating and using same 

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Patent Abstracts

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Notes

“The albumins (formed from Latin: albumen[3] "(egg) white; dried egg white") are a family of globular proteins, the most common of which is serum albumin. The albumin family consists of all proteins that are water-soluble, are moderately soluble in concentrated salt solutions, and experience heat denaturation.  Albumins are commonly found in blood plasma, and are unique from other blood proteins in that they are not glycosylated. Substances containing albumins, such as egg white, are called albuminoids.

A number of blood transport proteins are evolutionarily related, including serum albumin, alpha-fetoprotein, vitamin D-binding protein and afamin.

Albumin is the main protein of human plasma.  It binds water, cations (such as Ca2+, Na+ and K+), fatty acids, hormones, bilirubin, thyroxine (T4) and pharmaceuticals (including barbiturates) - its main function is to regulate the colloidal osmotic pressure of blood.  Alpha-fetoprotein (alpha-fetoglobulin) is a fetal plasma protein that binds various cations, fatty acids and bilirubin. Vitamin D-binding protein binds to vitamin D and its metabolites, as well as to fatty acids.  The biological role of afamin (alpha-albumin) has not yet been characterised.[

The 3D structure of human serum albumin has been determined by X-ray crystallography to a resolution of 2.5 Ĺ.

Albumin comprises three homologous domains that assemble to form a heart-shaped molecule.  Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. Structurally, the serum albumins are similar, each domain containing five or six internal disulfide bonds”

(Albumin, Wikipedia, 10/24/2013)

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Interested!!
Bookmark this page to follow future developments!.
(RDC 7/16/2012)

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Roger D. Corneliussen
Editor
www.maropolymeronline.com

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Tel: 610 363 9920
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E-Mail: cornelrd@bee.net  

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Copyright 2013 by Roger D. Corneliussen.
No part of this transmission is to be duplicated in any manner or forwarded by electronic mail without the express written permission of Roger D. Corneliussen
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* Date of latest addition; date of first entry is 10/8/2013.