Plasma preparation, human

Immunoglobulins are purified from the serum (or plasma) of human donors by methods similar to those used to purify animal-derived antibodies. In most instances, the immunoglobulin preparations are enriched in antibodies capable of binding to a specific antigen (usually an infectious mi-croorganism/virus). These may be purified from donated blood of individuals who have recently ... 

Tetanus antitoxin is routinely administered as part of the management of tetanus-prone wounds. The antibody preparation is purified from pooled serum/plasma of human donors who have been immunized with tetanus toxin. 

Holodniy M, Rainen L, Herman S, Yen-Lieberman B, Stability of plasma human immunodeficiency virus load in VACUTAINER PPT plasma preparation tubes during overnight shipment, J Clin Microbiol 2000 38 323-6. 

The acyl derivatives of kallikrein were prepared from porcine pancreatic kallikrein. In our experiments we used benzoyl-kallikrein. By deacylation the enzymatically active kallikrein was generated in plasma from benzoyl-kallikrein demonstrated by means of its amidolytic activity. From the time course of reactivation of benzoyl-kallikrein, a half-time of reactivation of 54 minutes was calculated. Benzoyl- kallikrein was protected from being inactivated by plasma inhibitors. Therefore, the kallikrein activity in plasma was higher after incubation with benzoyl-kallikrein than after incubation with the free enzyme. A comparatively high kinin activity was found in rabbit plasma. In human plasma, this effect was prevented by rapid degradation of kinin [42]. 

Detection of RDX in human and animal plasma and human urine and cerebrospinal fluid has been accomplished by HPLC/TEA and HPLC/UV (Army 1981a Fine et al. 1984 Turley and Brewster 1987). While both methods provide relatively rapid sample turn-around times, HPLC/TEA is the most sensitive and selective of the two, and requires little sample preparation (Fine et al. 1984). The older HPLC/UV method (Army 1981a) had the problem of coelution of a plasma component with the RDX peak. This was eradicated by clean-up on a cis bonded-phase extraction column (Turley and Brewster 1987 Woody et al. 1986), but the sensitivity of HPLC/UV was still several orders of magnitude less (CV). 

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. 

Experiments were also conducted using pooled human plasma. The predominant, stable form of the protein in plasma is prothrombin, a zymogen that is cleaved to yield the activated thrombin upon appropriate signaling (Blomback and Hanson, 1979). The presence of any detectable thrombin in its active (i.e., cleaved) form is probably due to stabilizers in the pooled plasma preparation. The plasma concentration of prothrombin is about 90mg/L (Blomback and Hanson, 1979), which corresponds to about 2.5 p.M, or 7.5 pmol on the aptamer spot. 

Human blood plasma contains over 700 different proteins (qv) (1). Some of these are used in the treatment of illness and injury and form a set of pharmaceutical products that have become essential to modem medicine (Table 1). Preparation of these products is commonly referred to as blood plasma fractionation, an activity often regarded as a branch of medical technology, but which is actually a process industry engaged in the manufacture of speciaUst biopharmaceutical products derived from a natural biological feedstock (see Pharmaceuticals). 

History. Methods for the fractionation of plasma were developed as a contribution to the U.S. war effort in the 1940s (2). Following pubHcation of a seminal treatise on the physical chemistry of proteins (3), a research group was estabUshed which was subsequendy commissioned to develop a blood volume expander for the treatment of military casualties. Process methods were developed for the preparation of a stable, physiologically acceptable solution of alburnin [103218-45-7] the principal osmotic protein in blood. Eady preparations, derived from equine and bovine plasma, caused allergic reactions when tested in humans and were replaced by products obtained from human plasma (4). Process studies were stiU being carried out in the pilot-plant laboratory at Harvard in December 1941 when the small supply of experimental product was mshed to Hawaii to treat casualties at the U.S. naval base at Pead Harbor. On January 5, 1942 the decision was made to embark on large-scale manufacture at a number of U.S. pharmaceutical plants (4,5). 

Spotnitz, W.D., Mintz, PD., Avery, N., Bithell, T.C., Kaul, S. and Nolan, S.P, Fibrin glue from stored human plasma An inexpensive and efficient method for local blood bank preparation. Am. Surg., 53, 460-464 (1987). 

R. Herraez-Heruandez, A. J. H. Eouter, N. C. van de Merbel and U. A. Th Brinkman, Automated on-line dialysis for sample preparation for gas cliromatogruphy determination of benzodiazepines in human plasma , 7. Pharm. Biomed. Anal. 14 1077-1087 (1996). 

The quantification of kinins in human tissues or body fluids has been limited due to the inherent difficulties in accurately measuring the concentration of ephemeral peptides. Today HPLC-based and RIA/capture-ELA measurements are established to determine kinins in human plasma, liquor or mine. Serine protease inhibitors need to be added to prevent rapid degradation of the kinins in vitro during sample preparation. Kinins and their degradation products have been studied in various biological milieus such as plasma/ serum, urine, joint fluids, kidney, lung and skeletal muscle [2]. Under normal conditions, the concentration of kinins in these compartments is extremely low for... 

In past years, treatment for patients with hemophilia A has consisted of administration of cryoprecipitates (enriched in factor VIII) prepared from individual donors or lyophilized factor VIII concentrates prepared from plasma pools of up to 5000 donors. It is now possible to prepare factor Vlll by recombinant DNA technology. Such preparations are free of contaminating viruses (eg, hepatitis A, B, G, or HlV-1) found in human plasma but are at present expensive their use may increase if cost of production decreases. 

Classically, to measure absolute absorption the plasma area imder the curve from an intravenous dose would be compared to that caused by the feeding of an oral dose. However, the carotenoids are lipid-soluble and are normally incorporated in chylomicrons synthesised in the enterocytes, a situation that cannot be replicated and applied to studies in humans because an intravenous preparation that would behave naturally is not possible. 

An LCD is a ubiquitous electronic display. Now, it is widely distributed among human daily life, like mobile phones, TV, and personal computers. The LCD has, however, a drawback, i.e., slower response than a plasma display or an electroluminescene display. Recently we have first succeeded in combination of a nanoparticle technology with the LCD technology, which realized fast response of the LCD [45,235,236]. Thus we have found a phenomenon, i.e., a frequency modulation of the LCD doped with metallic nanoparticles. Since the frequency modulation, or electro-optic property depends on the kind of metals, we have prepared AgPd bimetallic nanoparticles protected with a typical liquid crystal molecule, 4-cyano-4 -pentylbiphenyl (5CB) to investigate the electro-optic property [45,235,236]. 

Oncley, J.L., Gurd, F.R.N. and Melin, M. (1950). Preparation and properties of serum and plasma proteins XXV. Composition and properties on human serum d-lipoprotein. J. Am. Chem. Soc. 72, 458-464. 

Strancar, A., Barut, M., Podgomik, A., Koselj, P, Schwinn, H., Raspor, P, and Josic, D., Application of compact porous tubes from preparative isolation of clotting factor VII from human plasma, /. Chromatogr. A, 760, 117, 1997. 

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