Albumin structure

In recent years there has been a flurry of albumin sequence information, and now amino acid sequences have been deduced for several albumins as well as other members of the multigene family (Table I). The 

Aligned Albumin Sequences Illustrating Conserved Amino Acids and Invariant Residues SEQUENCE HOMOLOGY HUMAN/BOVINE/EQUINE/OVIMB/RAT/PROG/SAUmN 

IKTA aNBS FL XI SPHOaQB aTPT KTPDTAIiaxi. VTBl  

SRNL flAVQS SRSb aRVOT loBTb SKvas ISRSb anyeT 

AASg A baL STO TUA Asag uUiA ASTO AUtA IFN ARSK EAbA BHCQ KLHP SEBA EliVEV 

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J. R. Brown, R Shockley, Serum Albumin Structure and Characterization of Its Ligand Binding Sites , in Lipid-Protein Interactions , Eds. P. C. Jost, O. H. Griffith, Wiley, New York, 1982, Vol. 1, p. 25-68. 

Brown, J. R. 1977. Serum albumin Amino-acid sequence. In Albumin Structure, Function, and Uses. V.M. Rosenoer, M. Oratz and M.A. Rothschild (Editors). Pergamon Press, New York. 

McMenamy RH, Albumin binding sites, in Albumin Structure Function and Uses, Rosenoer VM, Oratz M, Rothschild MA (Eds.), Pergamon Press, Oxford, p. 143... 

Peters, T. Reed, R. G. In "Albumin Structure, Biosynthesis, Function ... 

Trypsin attacks the peptide bonds following the basic amino acids arginine and lysine. Formation of chloramines decrease trypsin binding sites, which causes a decrease in protein susceptibility to trypsin digestion. On the other hand, chloramine formation from free amino residues may induce changes in tertiary albumin structure, revealing some normally inaccessible amino residues. Therefore, removal... 

Peptide SYSM has no positively charged residue in its sequence. Labeling efficiency on this peptide was poor at pH 8.3. MPCAEDYLSWLN also contains no positively charged residue but this tyrosine was near a positively charged residue in the albumin structure. 

Over the years, albumin has been probed with diverse experimental methods, including hydrodynamics, low-angle X-ray scattering, fluorescence energy transfer, electrophoredc methods, and NMR, IR, UV, mass, and Raman spectroscopies. Virtually every measurable property has been determined more than once (Table IV), with each investigator seeking to establish important insight into albumin structure and chemistry. 

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