1977
DOI: 10.1111/j.1399-3011.1977.tb02784.x
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Isolation and Characterization of Highly Purified Alpha‐1‐antitrypsin

Abstract: Highly purified human alpha‐1‐antitrypsin (phenotype MM) was obtained by an original method of preparative electrophoresis. The criteria of homogeneity were assured by one arc in crossed immunoelectrophoresis and one band on polyacrylamide gel. A unique N‐terminal amino acid (pyroglutamic acid) and a unique C‐terminal residue (lysine) were identified. Determined by gel electrophoresis, its molecular weight was 47,000 daltons.

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Cited by 10 publications
(1 citation statement)
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“…In addition, Plancot et al [ 30 ] purified AAT by applying a complex procedure that consisted of five steps, the first of which was ammonium sulfate precipitation. Then, the material was loaded on Blue Dextran Sepharose 4 B followed by preparative electrophoresis, Con A Sepharose, and DEAE–cellulose chromatography.…”
Section: Methods Of Aat Purification: From the Beginning To The Prmentioning
confidence: 99%
“…In addition, Plancot et al [ 30 ] purified AAT by applying a complex procedure that consisted of five steps, the first of which was ammonium sulfate precipitation. Then, the material was loaded on Blue Dextran Sepharose 4 B followed by preparative electrophoresis, Con A Sepharose, and DEAE–cellulose chromatography.…”
Section: Methods Of Aat Purification: From the Beginning To The Prmentioning
confidence: 99%