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Publication : Structural comparisons between mouse and human prealbumin.

First Author  Wakasugi S Year  1985
Journal  J Biochem Volume  98
Issue  6 Pages  1707-14
PubMed ID  3005251 Mgi Jnum  J:14652
Mgi Id  MGI:62816 Doi  10.1093/oxfordjournals.jbchem.a135442
Citation  Wakasugi S, et al. (1985) Structural comparisons between mouse and human prealbumin. J Biochem 98(6):1707-14
abstractText  In an attempt to construct model systems for familial amyloidotic polyneuropathy, prealbumin cDNA was cloned from a mouse liver cDNA library, using previously cloned human prealbumin cDNA as a hybridization probe. The primary structure of mouse prealbumin deduced from the cDNA sequence shows that it consists of 147 amino acids, including a whole prealbumin sequence (127 amino acids) and a putative signal sequence (20 amino acids). These numbers are in complete agreement with those determined for the human prealbumin. Among the 127 amino acid residues of the mature human prealbumin, 25 are replaced by different amino acids in the mouse prealbumin. Interestingly, 24 out of the 25 substituted amino acids are located at the outer surface of the protein, and the regions corresponding to the core and central channel of the protein are almost completely conserved. The cloned cDNA provided essential information for manipulating amyloidosis in mice.
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