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Origin of the multiple components of human α1-antitrypsin

✍ Scribed by Akira Yoshida; Mia Wessels

Publisher
Springer
Year
1978
Tongue
English
Weight
389 KB
Volume
16
Category
Article
ISSN
0006-2928

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✦ Synopsis

Multiple components of human el-antitrypsin were separated by preparative starch gel electrophoresis, and the sialic acid contents of these components were determined. The acidic components contained more sialic acid per molecule than the basic components. The molecular sizes of these components were identical, excluding the possibility of polymerization of the inhibitor in the formation of the multiple components. Consequently, the multiple components of the inhibitor are primarily due to differences in the sialic acid content of each component. Three major components contain eight, seven, and six sialic acid residues per molecule, respectively.

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Glycosylation of human α1-antitrypsin inSaccharomyces cerevisiae and methylotrophic yeasts
✍ Kang, Hyun Ah; Sohn, Jung-Hoon; Choi, Eui-Sung; Chung, Bong Hyun; Yu, Meyong-Hee 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 211 KB

Human alpha 1-antitrypsin (alpha 1-AT) is a major serine protease inhibitor in plasma, secreted as a glycoprotein with a complex type of carbohydrate at three asparagine residues. To study glycosylation of heterologous proteins in yeast, we investigated the glycosylation pattern of the human alpha 1