Isolation by zinc-affinity chromatography of the histidine–proline-rich-glycoprotein molecule associated with rabbit skeletal muscle AMP deaminase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry
Reference34 articles.
1. Histidine-rich glycoprotein modulation of the anticoagulant activity of heparin. Evidence for a mechanism involving competition with both antithrombin and thrombin for heparin binding.
2. Domain Structure and Conformation of Histidine−Proline-Rich Glycoprotein,
3. Association of purified skeletal-muscle AMP deaminase with a histidine–proline-rich-glycoprotein-like molecule
4. Presence in Human Skeletal Muscle of an AMP Deaminase-associated Protein That Reacts with an Antibody to Human Plasma Histidine-Proline-rich Glycoprotein
5. Regulation of skeletal muscle AMP deaminase effects of limited proteolysis on the activity of the rabbit enzyme
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