Biochemical properties and possible therapeutic role of the elastase inhibitor eglin C. 1985

H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider

UI MeSH Term Description Entries
D007865 Leeches Annelids of the class Hirudinea. Some species, the bloodsuckers, may become temporarily parasitic upon animals, including man. Medicinal leeches (HIRUDO MEDICINALIS) have been used therapeutically for drawing blood since ancient times. Hirudinea,Hirudineas,Leeche
D007962 Leukocytes White blood cells. These include granular leukocytes (BASOPHILS; EOSINOPHILS; and NEUTROPHILS) as well as non-granular leukocytes (LYMPHOCYTES and MONOCYTES). Blood Cells, White,Blood Corpuscles, White,White Blood Cells,White Blood Corpuscles,Blood Cell, White,Blood Corpuscle, White,Corpuscle, White Blood,Corpuscles, White Blood,Leukocyte,White Blood Cell,White Blood Corpuscle
D010196 Pancreatic Elastase A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36. Elastase,Pancreatopeptidase,Elastase I,Pancreatic Elastase I,Elastase I, Pancreatic,Elastase, Pancreatic
D011480 Protease Inhibitors Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES). Antiprotease,Endopeptidase Inhibitor,Endopeptidase Inhibitors,Peptidase Inhibitor,Peptidase Inhibitors,Peptide Hydrolase Inhibitor,Peptide Hydrolase Inhibitors,Peptide Peptidohydrolase Inhibitor,Peptide Peptidohydrolase Inhibitors,Protease Antagonist,Protease Antagonists,Antiproteases,Protease Inhibitor,Antagonist, Protease,Antagonists, Protease,Hydrolase Inhibitor, Peptide,Hydrolase Inhibitors, Peptide,Inhibitor, Endopeptidase,Inhibitor, Peptidase,Inhibitor, Peptide Hydrolase,Inhibitor, Peptide Peptidohydrolase,Inhibitor, Protease,Inhibitors, Endopeptidase,Inhibitors, Peptidase,Inhibitors, Peptide Hydrolase,Inhibitors, Peptide Peptidohydrolase,Inhibitors, Protease,Peptidohydrolase Inhibitor, Peptide,Peptidohydrolase Inhibitors, Peptide
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D001798 Blood Proteins Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins. Blood Protein,Plasma Protein,Plasma Proteins,Serum Protein,Serum Proteins,Protein, Blood,Protein, Plasma,Protein, Serum,Proteins, Blood,Proteins, Plasma,Proteins, Serum
D004797 Enzyme-Linked Immunosorbent Assay An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed. ELISA,Assay, Enzyme-Linked Immunosorbent,Assays, Enzyme-Linked Immunosorbent,Enzyme Linked Immunosorbent Assay,Enzyme-Linked Immunosorbent Assays,Immunosorbent Assay, Enzyme-Linked,Immunosorbent Assays, Enzyme-Linked
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D015843 Serpins A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition but differ in their specificity toward proteolytic enzymes. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES. Serpin,Serpin Superfamily,Serpin Peptidase Inhibitors,Serpin Protease Inhibitors,Inhibitors, Serpin Peptidase,Inhibitors, Serpin Protease,Peptidase Inhibitors, Serpin,Protease Inhibitors, Serpin,Superfamily, Serpin

Related Publications

H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider
March 1992, Circulatory shock,
H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider
June 1989, Journal of molecular biology,
H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider
January 1986, European journal of respiratory diseases. Supplement,
H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider
March 1992, Biological chemistry Hoppe-Seyler,
H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider
November 1987, Biological chemistry Hoppe-Seyler,
H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider
January 1990, Experimental lung research,
H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider
May 1988, Biological chemistry Hoppe-Seyler,
H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider
July 2008, Journal of medical microbiology,
H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider
April 1987, Biological chemistry Hoppe-Seyler,
H P Schnebli, and U Seemüller, and H Fritz, and R Maschler, and M Liersch, and J L Bodmer, and G D Virca, and E C Lucey, and P G Stone, and G L Snider
January 1991, Chemical & pharmaceutical bulletin,
Copied contents to your clipboard!