Inter-alpha-trypsin-inhibitor (ITI): two distinct mRNAs in baboon liver argue for a discrete synthesis of ITI and ITI derivatives
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(83)80791-1/fullpdf
Reference18 articles.
1. Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, III. Sequence of the two Kunitz-Type Domains inside the Native Inter-α-Trypsin Inhibitor, Its Biological Aspects and also of Its Cleavage Products
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2. The Inter-α-Trypsin Inhibitor Family: Versatile Molecules in Biology and Pathology;Journal of Histochemistry & Cytochemistry;2020-07-08
3. Inter-α-trypsin Inhibitor, a Covalent Protein-Glycosaminoglycan-Protein Complex;Journal of Biological Chemistry;2004-09
4. Human myometrial cells in culture express specific binding sites for urinary trypsin inhibitor;Molecular Human Reproduction;2000-08-01
5. Inter-alpha-trypsin inhibitor proteoglycan family. A group of proteins binding and stabilizing the extracellular matrix;European Journal of Biochemistry;1998-03-15
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