Selective proteolysis of ovine lutropin or its beta subunit by endoproteinase Arg-C. Properties of the Arg beta 43 cleaved hormone.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
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1. The catalytic domain of site-specific recombinase;Proceedings of the National Academy of Sciences;1997-06-10
2. hCG-receptor binding and transmembrane signaling;Molecular and Cellular Endocrinology;1996-12
3. Human follitropin heterodimerization and receptor binding structural motifs: identification and analysis by a combination of synthetic peptide and mutagenesis approaches;Molecular and Cellular Endocrinology;1996-12
4. Circular dichroic spectroscopy of Arg46-nicked ovine lutropin α and derived fragments;Journal of Protein Chemistry;1996-08
5. The Groove between the α- and β-Subunits of Hormones with Lutropin (LH) Activity Appears to Contact the LH Receptor, and Its Conformation Is Changed during Hormone Binding;Journal of Biological Chemistry;1995-08
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