Volume 10, Issue 2 pp. 113-119
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ISOLATION AND CHARACTERIZATION OF HIGHLY PURIFIED ALPHA-1-ANTITRYPSIN

Marie-Therese Plancot

Marie-Therese Plancot

Laboratoire des Protéines Fibreuses, Unité nd̀16 de l'INSERM, Lille Cédex, France

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Andre Delacourte

Andre Delacourte

Laboratoire des Protéines Fibreuses, Unité nd̀16 de l'INSERM, Lille Cédex, France

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Dr. Kia-Ki Han

Corresponding Author

Dr. Kia-Ki Han

Laboratoire des Protéines Fibreuses, Unité nd̀16 de l'INSERM, Lille Cédex, France

Laboratoire des Protéines Fibreuses Unité nd̀ 16 de l'INSERM Place de Verdun 59045 Lille Cédex FranceSearch for more papers by this author
Michel Dautrevaux

Michel Dautrevaux

Laboratoire des Protéines Fibreuses, Unité nd̀16 de l'INSERM, Lille Cédex, France

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Gerard Biserte

Gerard Biserte

Laboratoire des Protéines Fibreuses, Unité nd̀16 de l'INSERM, Lille Cédex, France

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First published: August 1977
Citations: 9

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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