Assay of Complexed a1 -Antichymotrypsin in Plasma

1. Rash JM, Jerkunica I, Sgoutas DS. Lipid interference in steroid radioimniunoassay. Cliii Chem 1980;26:84-8. 2. Rash JM, Jerkunica I, Sgoutas DS. Mechanisms of interference of non-esterifled fatty acids in radioimmunoassays of steroids. Cliii Chim Acta 1979;93:283-94. 3. Andersen KJ, Schjonsby H, Skagen DW, von der Lippe G. Bile acid and detergent interaction with radioassays based on coated charcoal. Cliii Chem 1976;22:1727-8. 4. Andersen KJ, von der Lippe G, Schjonsby H. Bile and detergent interaction with the radioasaay for vitamin B12 binders using protein and dextran-covered charcoal. Anal Biochem 1976;74:48895. 5. Shaw W, Powell MK, Bayse D. The influence of serum albumin concentration on fatty acid interference in the radioimmunoassay (RIA) for serum digoxin [Abstract]. Clin Chem 1977;22:1124-5. 6. Weltzien HU. Cytolytic and membrane perturbing properties of lysophosphatidyichohne. Biochini Biophys Acts 1979;559:259-87. 7. Switzer 5, Eder HA. Transport of lysolecithin by albumin in human and rat plasma. J Lipid Res 1965;6:506-1l. 8. Diem K, Lentner C, eds. Scientific tables, 7th ed. Basle: Documenta Geigy, 1970:604. 9. Vadas P, Pruzanski W. Biology of disease, role of secretory phospholipase A2 in the pathobiology of disease. Lab Invest 1986;55:391-404. 10. Chung J, Ahano R, Byrne R, Scandu AM. In vitro mass: activity distribution of lecithin-cholesterol acyltransferase among human plasma lipoproteuns. Atherosclerosis 1982;45:33-41.

[1]  D. Perlmutter,et al.  The SEC receptor recognizes a pentapeptide neodomain of α1-antitrypsin-protease complexes , 1991 .

[2]  K. Ohlsson,et al.  Release of dog polymorphonuclear leukocyte cathepsin G, normally and in endotoxin and pancreatitic shock. Isolation and partial characterization of dog polymorphonuclear leukocyte cathepsin G. , 1991, Biological chemistry Hoppe-Seyler.

[3]  J. Enghild,et al.  Analysis of the plasma elimination kinetics and conformational stabilities of native, proteinase-complexed, and reactive site cleaved serpins: comparison of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, antithrombin III, alpha 2-antiplasmin, angiotensinogen, and ovalbumin. , 1991, Biochemistry.

[4]  D. Perlmutter,et al.  The SEC receptor recognizes a pentapeptide neodomain of alpha 1-antitrypsin-protease complexes. , 1991, The Journal of biological chemistry.

[5]  U. Stenman,et al.  A complex between prostate-specific antigen and alpha 1-antichymotrypsin is the major form of prostate-specific antigen in serum of patients with prostatic cancer: assay of the complex improves clinical sensitivity for cancer. , 1991, Cancer research.

[6]  K. Misono,et al.  Identification of a highly specific chymase as the major angiotensin II-forming enzyme in the human heart. , 1990, The Journal of biological chemistry.

[7]  J. Travis,et al.  Acute phase protein stimulation by alpha 1-antichymotrypsin-cathepsin G complexes. Evidence for the involvement of interleukin-6. , 1990, The Journal of biological chemistry.

[8]  K. Havemann,et al.  Assay of functional activity of alpha 1-antichymotrypsin in plasma. , 1990, Clinical chemistry.

[9]  H. Lilja,et al.  Enzymatic activity of prostate-specific antigen and its reactions with extracellular serine proteinase inhibitors. , 1990, European journal of biochemistry.

[10]  B. Cooperman,et al.  Reaction of human skin chymotrypsin-like proteinase chymase with plasma proteinase inhibitors. , 1989, The Journal of biological chemistry.

[11]  J. Mcdonald Mammalian Proteases : A Glossary and Bibliography , 1986 .

[12]  S. Neumann,et al.  “PMN-Elastase Assay”: Enzyme Immunoassay for Human Polymorphonuclear Elastase Complexed with α1-Proteinase Inhibitor , 1984, Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie.

[13]  G. Salvesen,et al.  Human plasma proteinase inhibitors. , 1983, Annual review of biochemistry.

[14]  R. Hirschelmann,et al.  Some effects of lysolecithin in vivo and in vitro and their possible relations to the inflammatory process. , 1982, Agents and actions. Supplements.

[15]  P. Broughton,et al.  International Federation of Clinical Chemistry, Scientific Committee Expert Panel on Nomenclature and Principles of Quality Control in Clinical Chemistry. Approved recommendation (1979) on quality control in clinical chemistry. Part 3. Calibration and control materials. , 1980, Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie.

[16]  J. Travis,et al.  Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. , 1980, The Journal of biological chemistry.

[17]  N. Heimburger,et al.  Charakterisierung von α1 X-glykoprotein als chymotrypsin-lnhibitor des humanplasmas , 1965 .