Low molecular weight serine proteinase inhibitors of human articular cartilage. Isolation, Characterization, and Biosynthesis
Author:
Publisher
Wiley
Subject
Pharmacology (medical),Immunology,Rheumatology,Immunology and Allergy
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1. Binding of SPAAT, the 44-residue C-terminal peptide of alpha 1-antitrypsin, to proteins of the extracellular matrix;J CELL BIOCHEM;1997
2. Binding of SPAAT, the 44-residue C-terminal peptide of α1-antitrypsin, to proteins of the extracellular matrix;Journal of Cellular Biochemistry;1997-09-01
3. Inhibition of human serine proteases by SPAAT, the C-terminal 44-residue peptide from α1-antitrypsin;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1997-06
4. Purification, Characterization, and Biosynthesis of Bovine Cartilage Lysozyme Isoforms;Archives of Biochemistry and Biophysics;1997-03
5. Distribution of the Secretory Leucocyte Proteinase Inhibitor in Human Articular Cartilage;Biological Chemistry;1997-01-01
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