Immunoaffinity purification of calpastatin and calpastatin constructs
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference34 articles.
1. Purification and Characterization of an Inhibitor of Calcium- Activated Neutral Protease from Rabbit Skeletal Muscle
2. The appearance of a 34,000-dalton inhibitor of calpain (Ca2+-dependent cysteine proteinase) in rat liver after the administration of phenylhydrazine
3. Purification and Characterization of an Inhibitor of Calcium-Activated Neutral Protease from Rabbit Skeletal Muscle: Purification of 50,000-Dalton Inhibitor
4. Purification and Characterization of 210,000-Dalton Inhibitor of Calcium-Activated Neutral Protease from Rabbit Skeletal Muscle and Its Relation to 50,000-Dalton Inhibitor
Cited by 7 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. Submitochondrial localization of associated μ-calpain and calpastatin;Archives of Biochemistry and Biophysics;2008-02
2. Purification and characterization of calpain and calpastatin from rainbow trout, Oncorhynchus mykiss;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;2007-04
3. Differential tissue expression of a calpastatin isoform in Xenopus embryos;Micron;2007-04
4. Expression and immunolocalization of the calpain–calpastatin system during parthenogenetic activation and fertilization in the rat egg;Reproduction;2006-01
5. The Calpain System;Physiological Reviews;2003-07
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