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Spectral studies on 2 genetic forms of the human serum proteinase inhibitor alpha 1 anti trypsin


, : Spectral studies on 2 genetic forms of the human serum proteinase inhibitor alpha 1 anti trypsin. International Journal of Peptide and Protein Research 12(5): 284-292

Alpha-1-antitrypsin, the major inhibitor of proteolytic enzymes in human serum, was isolated from normal individuals (protease inhibitor type MM) and from those with an inherited deficiency (protease inhibitor type ZZ) of circulatory protein. The 2 proteins were compared by circular dichroism spectroscopy, and by fluorescence quenching experiments using anionic (I-), and neutral (acrylamide) probes. Both proteins share a similar secondary structure, i.e. .apprx. 45-50% .alpha.-helix and 15-20% .beta.-structure. The microenvironment in the vicinity of the 3 tryptophanyl residues is apparently altered in Z form as compared to the M form as shown by the absence of the positive dichroic band in the region 290-300 nm of the circular dichroism spectra, a > 50% increase in quantum yield in the tryptophanyl fluorescence emission spectra, an increased accessibility of tryptophan to quenching by iodide, and acrylamide quenching experiments which indicate that all tryptophanyl residues in the Z protein are quenched equally or that quenching is dominated by a single residue, while in the M protein, heterogenous quenching occurs. The potential significance of these findings in terms of alpha-1-antitrypsin deficiency state are discussed.

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