Molecular cloning and bacterial expression of cDNA for rat calpain II 80 kDa subunit
- 1 October 1993
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression
- Vol. 1216 (1), 81-93
- https://doi.org/10.1016/0167-4781(93)90040-k
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin?BioEssays, 1992
- Constitutive expression of calpain II in the rat uterus during pregnancy and involutionBiochemical Journal, 1991
- Analysis of Calcium-Binding Sites in Calcium-Activated Neutral ProteasePublished by Springer Nature ,1989
- [25] Primer extension analysis of RNAMethods in Enzymology, 1989
- Molecular cloning of the cDNA for the large subunit of the high-calcium-requiring form of human calcium-activated neutral proteaseBiochemistry, 1988
- Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA PolymeraseScience, 1988
- Complete amino acid sequence of the large subunit of the low‐Ca2+‐requiring form of human Ca2+‐activated neutral protease (μCANP) deduced from its cDNA sequenceFEBS Letters, 1986
- Gene structure of calcium‐dependent protease retains the ancestral organization of the calcium‐binding protein geneFEBS Letters, 1986
- Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?Nature, 1984
- Ca2+-activated proteinase in the rat. Quantification by immunoassay in the uterus during pregnancy and involution, and in other tissuesBiochemical Journal, 1984