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Serum alpha -antitrypsin

PPL Therapeutics Bile human gastric Lipase, Fibrinogen, thrombin, Factor VII, Factor IX, alpha-antitrypsin, calcitonin (salmon), collagen, superoxide dismutase, Glucagon lipopeptide, Human serum albumin, Protein C 59-63... [Pg.837]

Fig. 1.2. Long-term expression of a rAAV2 vector after delivery to mouse liver. Aliquots of the indicated dosages of a CMV enhancer/chicken beta actin hybrid promoter-driven human alpha 1-antitrypsin (AAT)-expressing rAAV2 vector (CB-AT) or of a similar elongation factor 1-alpha promoter-driven vector (E-AT) were injected into C57B1/6 mice either by portal vein (PV) or tail vein (TV). The serum levels of human AAT were measured by ELISA serially from 0 to 52 weeks after injection, and these values are shown on the y-axis. Fig. 1.2. Long-term expression of a rAAV2 vector after delivery to mouse liver. Aliquots of the indicated dosages of a CMV enhancer/chicken beta actin hybrid promoter-driven human alpha 1-antitrypsin (AAT)-expressing rAAV2 vector (CB-AT) or of a similar elongation factor 1-alpha promoter-driven vector (E-AT) were injected into C57B1/6 mice either by portal vein (PV) or tail vein (TV). The serum levels of human AAT were measured by ELISA serially from 0 to 52 weeks after injection, and these values are shown on the y-axis.
Song, S., Laipis, P., Embury, J., Berns, K., Crawford, J. and Flotte, T. R. (2001b). Stable therapeutic serum levels of human alpha-1 antitrypsin (AAT) after portal vein injection of recombinant adeno-associated virus (rAAV) vectors. Gene Ther. 8, 1299-1306. [Pg.17]

The fecal clearance of alpha-1-antitrypsin (AT) can also be used as a marker of GI protein loss. AT is a glycoprotein (MW 54,000) that is synthesized in the fiver and is normally present in the serum at a concentration of about 1.5 to 2 g/L. It is a protease inhibitor and therefore resistant to degradation by proteolytic enzymes in the GI tract. The fecal clearance of AT correlates with protein loss measured by Cr techniques (r = 0.96). The correlation is not influenced by serum AT concentrations or by fecal weight. AT clearance can be used for both small and large bowel disease and is appficable to the evaluation of enteric protein loss in children or adults.More recent work has confirmed these findings and also confirmed that fecal AT concentration alone does not reliably predict AT clearance (i.e., a timed fecal sample and measurement of serum AT is required). An important observation is that experimentally induced diarrhea in normal subjects leads to an increased AT clear-... [Pg.1866]

C.-B. Laurell and S. Eriksson. The electrophoretic alpha 1-globulin pattern of serum in alpha 1-antitrypsin deficiency. Scand. J. Lab. Clin. Med. 75 132 (1963). [Pg.327]

Simple systems (with a single defined additive) were produced with each of the following materials. Calf thymus DNA, polymerized, was obtained from Sigma. Protein sources were prepared in-house and subsequently dialyzed into low salt solutions. Human serum albumin and immunoglobulin G (IgG) were plasma-derived. Human immunoglobulin M (IgM) was produced by tissue culture fermentation and purified. A defined complex system consisted of both albumin and IgM together. An undefined complex system was set up with an intermediate material of Cohn plasma fractionation containing alpha-1 antitrypsin (alpha-1), albumin, and other contaminants. [Pg.97]

Alpha 1-antitrypsin deficiency Patients with deficiency of the protease inhibitor, alpha 1-antitrypsin, may present with liver disease in childhood or with pulmonary emphysema in adults. All patients with genotypes associated with low alpha 1-antitrypsin in the serum are likely to develop emphysema if they smoke or are exposed to environmental pollutants... [Pg.62]

A novel foetal polypeptide, characterised by an apparent Mr of 46 000 and a p7 of 5.0 was identified. N-terminal microsequencing (25-EDPQ) and immunoblotting using specific anti-alpha-l-antitr3tpsin antibodies reveal that this spot most likely corresponds to a foetal specific form of alpha-1-antitrypsin (Tissot et al, 2000b). The polypeptide was observed in all foetal samples and in all plasma/serum samples obtained from infants of less than 2... [Pg.72]

One, rare, mechanism by which it may arise is a defect of glycosylation of alpha-1-antitrypsin, leading to its premature clearance from serum and consequent depletion in the lung and elsewhere. [Pg.295]

Protein Growth velocity, serum liver enzyme levels, liver size by examination Urine and serum amino acid levels, serum glucose serum proteins (e.g., albumin, prealbumin, clotting factors, alpha-l-antitrypsin, transferrin), serum liver enzyme levels, liver size by examination and ultrasound... [Pg.115]

Sensitized cells release specific cytokine and chemokine mediators that can be quantified. These include substances such as histamine and tryptase, as well as markers of inflammation in the gastrointestinal tract. The latter may be of value in the evaluation of allergic response since inflammation is a risk factor for increased sensitization. Markers of intestinal inflammation include eosinophil cationic protein in serum and feces, a-1 antitrypsin, and tumor necrosis factor alpha (Majamaa et ak, 1996). Skin prick and patch tests have good negative predictive value, but poor positive predictive value, and therefore are of more limited use in clinical testing. [Pg.123]

Dolitzky, Y., Sturchak, S., Nizan, B., Sela, B.A., and Margel, S. (1994). Synthesis, characterization, and use of immobilized polyacrolein microspheres in diagnostics—a model determination of alpha) 1 )-antitrypsin in human serum. Analyt. Biochem. 220 (2), 257-267. [Pg.373]


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