Isolation and characterization of two minor fractions of α1,-antitrypsin by high-performance liquid chromatographic chromatofocusing

Jan olof Jeppsson, Hans Lilja, Maria Johansson

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

Sammanfattning

α1-Antitrypsin is a glycoprotein that separates into five electrophoretic fractions, viz. M2, M4, M6, M7 and M8. Con A-Sepharose separates the protein into three fractions according to the branching degree of the three oligosaccharide chains. The Con A affinity is identical for M4 and M7 and for M6 and M8. Within each pair the proteins were isolated by rapid chromatofocusing. The M7 and M8 have the same carbohydrate structure as the major M4 and M6 respectively, but have lost the first five N-terminal amino acids (Glu-Asp-Pro-Glu-Gly) as compared to the majority of the protein.

Originalspråkengelska
Sidor (från-till)173-177
TidskriftJournal of Chromatography A
Volym327
DOI
StatusPublished - 1985 juni 26

Ämnesklassifikation (UKÄ)

  • Biologi

Fingeravtryck

Utforska forskningsämnen för ”Isolation and characterization of two minor fractions of α1,-antitrypsin by high-performance liquid chromatographic chromatofocusing”. Tillsammans bildar de ett unikt fingeravtryck.

Citera det här