Isolation and characterization of the cyanogen bromide glycopeptide fragments of alpha-1-antitrypsin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference25 articles.
1. Molecular abnormality of human alpha1-antitrypsin variant (Pi-ZZ) associated with plasma activity deficiency.
2. Molecular basis for the α1-protease inhibitor deficiency
3. Comparison of the chemical, physical, and survival properties of normal and Z-variant alpha-1-antitrypsins.
Cited by 6 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Uniformity of Glycans within Molecular Variants of αl-Protease Inhibitor with Distinct Affinity for Concanavalin A;European Journal of Biochemistry;2005-03-03
2. α-1-Antitrypsin metabolism in the protein-deficient weanling rat;British Journal of Nutrition;1985-07
3. Comparison of the hydrolysis and the covalent binding of 6-diazo-5-oxo-l-[6-14C]norleucine by rat renal phosphate-dependent glutaminase;Archives of Biochemistry and Biophysics;1982-01
4. Isolation and characterization of rat alpha-1-antitrypsin.;Journal of Biological Chemistry;1981-08
5. Studies on the oligosaccharide chains of human alpha 1-protease inhibitor. I. Isolation of glycopeptides.;Journal of Biological Chemistry;1980-05
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