Globulin, blood plasma

A method for the fractionation of plasma, allowing albumin, y-globulin, and fibrinogen to become available for clinical use, was developed during World War II (see also Fractionation, blood-plasma fractionation). A stainless steel blood cell separation bowl, developed in the early 1950s, was the earhest blood cell separator. A disposable polycarbonate version of the separation device, now known as the Haemonetics Latham bowl for its inventor, was first used to collect platelets from a blood donor in 1971. Another cell separation rotor was developed to faciUtate white cell collections. This donut-shaped rotor has evolved to the advanced separation chamber of the COBE Spectra apheresis machine. 

Primary blood components iaclude plasma, red blood cells (erythrocytes), white blood cells (leukocytes), platelets (thrombocytes), and stem cells. Plasma consists of water dissolved proteias, ie, fibrinogen, albumins, and globulins coagulation factors and nutrients. The principal plasma-derived blood products are siagle-donor plasma (SDP), produced by sedimentation from whole blood donations fresh frozen plasma (FFP), collected both by apheresis and from whole blood collections cryoprecipitate, produced by cryoprecipitation of FFP albumin, collected through apheresis and coagulation factors, produced by fractionation from FFP and by apheresis (see Fractionation, blood-plasma fractionation). 

Immune Globulin (IG) IG is a sterile solution containing antibodies from human blood. It is obtained by cold ethanol fractionation of large pools of blood plasma and contains 15-18 percent protein. Intended for intramuscular administration, IG is primarily indicated for routine maintenance of immunity of certain immunodeficient persons and for passive immunity against measles and hepatitis. IG does not transmit hepatitis B virus, human immunodeficiency virus (HIV), or other infectious diseases. 

Intravenous Immune Globulin (IGIV) IGIV is a product derived from blood plasma from a donor pool similar to the immune globulin (IG) pool, but prepared so it is suitable for intravenous use. IGIV does not transmit infectious diseases. It is primarily used for replacement therapy in primary antibody-deficiency disorders, for the treatment of Kawasaki disease, immune thrombocytopenic purpura, hypogammaglobulinemia in chronic lymphocytic leukemia, and in some cases of HIV infection. 

Antibodies are members of a group of proteins known collectively as immunoglobulins. The name is derived from the observation that during electrophoresis of blood plasma the proteins associated with antibody activity migrate with the gamma globulin fraction. 

Some 100 different proteins occur in human blood plasma. Based on their behavior during electrophoresis (see below), they are broadly divided into five fractions albumins and ai-, tt2-, P- and y-globulins. Historically, the distinction between the albumins and globulins was based on differences in the proteins solubility -albumins are soluble in pure water, whereas globulins only dissolve in the presence of salts. 

The table also lists important globulins in blood plasma, with their mass and function. The a- and p-globulins are involved in the transport of lipids (lipoproteins see p. 278), hormones, vitamins, and metal ions. In addition, they provide coagulation factors, protease inhibitors, and the proteins of the complement system (see p. 298). Soluble antibodies (immunoglobulins see p. 300) make up the y-globulin fraction. 

GAMMA GLOBULIN. The fraction of the protein globulins of the blood plasma in which are found the antibodies. 

The stability of such HCP is not high. For instance, although the heparin (ionic bonds) — ternary ammonium salts (covalent bonds) — polypropylene associate is not actually affected by distilled water, the 3 hours storage of the product in blood plasma reduces the surface concentration of heparin to 30% of its initial value65. It is noteworthy that heparin is very effectively eluted by solutions of y-globuline (Table 7)65>. 

Al. Abdel-Wahab, E. M., Rees, V. H., and Laurence, D. J. R., Evaluation of the albumin-globulin ratio of blood plasma or serum by paper electrophoresis. In Paper Electrophoresis, Ciba Foundation Symposium (G. E. W. Wolstenholme and E. C. P. Millar, eds.), pp. 30-39. Churchill, London, 1958. 

Plasma kinins are tissue hormones liberated from a-globulins of the blood plasma by kallikrein. 

Boettcher, E. W., P. Kistler, and H. Nitschmann Method of isolating the beta -metal-combining globulin from human blood plasma. Nature 181, 490 (1958). 

Heparin can be attached to a variety of surfaces by means of complex formation with quaternary ammonium salts. Depending on the method used to attach heparin, the resulting surfaces may or may not release heparin when contacted with blood plasma. The removal of heparin from surfaces by plasma protein fractions was studied and it was found that alpha-globulins removed greater amounts than any other fraction. Heparinized surfaces adsorb proteins when exposed to blood or plasma. However, with the possible exception of thrombin, there is no consistent pattern of protein adsorption which can be related to their nonthrombogenicity. 

The most commonly biopolymers separated by Fl-FFF are proteins [49]. Fl-FFF is capable of separating proteins differing by just 15% in size within 3 to 10 min. S-Fl-FFF has been applied to a variety of proteins, including albumin, ovalbumin, y-globulin, hemoglobin, ferritin, lysozyme, [1-casein, apoferritin, human and rat blood plasmas and elastin [41,240,247]. Fl-FFF was also used to investigate the structural transformations of proteins [240]. 

It must be pointed out that the so-called quasi-albumins described by Poulik and Smithies (P13) are immunologically unrelated to albumin and would be more appropriately named quasi-oi-globulins. These proteins migrate just behind albumin in the vertical starch-gel electrophoretic technique of Smithies (S34) and include the group-specific (Gc) components. A fetal plasma protein of similar electrophoretic mobility is known (B12, B13), whose carbohydrate content is 23 mg/g, which clearly distinguishes it from the glycoprotein fetuin. Occasionally the protein persists and can be observed in some neonatal blood plasmas. 

The (3-globulins represent 13% of the blood plasma proteins and include transferrin (an iron transport protein) and low-density lipoprotein. Fibrinogen, a protein involved in coagulation of blood, comprises 7% of the plasma protein. Finally, the 7-globulins, IgG, IgM, IgA, IgD, and IgE, make up the remaining 11% of the plasma proteins. The 7-globuUns are synthesized by B lymphocytes, but most of the remaining plasma proteins are synthesized in the liver. In fact, a frequent hallmark of liver disease is reduced amounts of one or more of the plasma proteins. 

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