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PMID: 6980014 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Locations of oligosaccharide chains in human alpha 1-protease inhibitor and oligosaccharide structures at each site.

Biochemistry ·Vol. 21 ·No. 11 ·1982-05-25 ·Pages 2805-10

Hodges LC, Chan SK

Abstract

Previous studies in this laboratory had shown that the alpha 1-protease inhibitor (alpha 1-PI) molecule contained two types of oligosaccharides, biantennary and triantennary. Cleavage of human alpha 1-protease inhibitor with CNBr resulted in three carbohydrate-containing fragments, I-III. Composition data revealed that each of these CNBr fragments contained one oligosaccharide chain. The oligosaccharide structure at each glycosylation site on each purified CNBr fragment was determined by compositional analysis, behavior on Con A affinity chromatography, and methylation analysis. From the results of these studies, we propose that fragment I contains one carbohydrate chain that can be of either the biantennary or triantennary type. On the other hand, fragments II and III each contain one carbohydrate chain exclusively by the biantennary type of complex N-glycoside.

MeSH Terms
Amino Acids/analysis Blood Proteins/analysis Carbohydrates/analysis Cyanogen Bromide Humans Oligosaccharides/analysis Peptide Fragments/analysis alpha 1-Antitrypsin
Chemicals
Amino Acids Blood Proteins Carbohydrates Oligosaccharides Peptide Fragments alpha 1-Antitrypsin Cyanogen Bromide
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hodges L C
Chan S K
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1982-05-25
Pages
2805-10
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Grants
NHLBI NIH HHS · HL-16166 · United States
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