research on electrophoresis and adsorption analysis, especially for his discoveries concerning the complex nature of the serum proteins
Serum proteins as health and nutrition indicators
The protein composition of blood responds over the time period of days to weeks to changes in diet as well as inflammatory and infectious disease. Plasma can be similarly analyzed.
Total serum protein is the sum of the individual fractions measured separately (discussed below) as well as the collection of a diversity of proteins found in relatively low concentration. The total serum protein concentration is used in a correlation analysis with albumin, IgG and acute phase proteins. If serum protein concentration is elevated but uncorrelated with an specific fraction then it idicates that the individual is dehydrated from water stress. Typically, total serum protein concentration is correlated with increased concentrations of albumin, IgG and/or acute phase proteins. [Measured in 2 ul of serum using Coomassie R-250 dye binding and spectrophotometry]
Albumin is the most abundant protein in serum and is synthesized by the liver to maintain homostatic levels when protein intake is sufficient. Decreased albumin concentration, which is typically correlated with decreased total protein concentration, indicates protein malnutrition. Depending on the composition of the diet, decreased albumin may indicate energy malnutrition whereby proteins are catabolized for gluconeogenesis. [Measured in 3 ul of serum by bromcresol-green dye binding and spectrophotometry]
Immunoglobulin G (IgG) is the second most abundant protein in plasma and is synthesized by B-lymphocytes in response to the sum of immunogenic stimulation. The levels of IgG are decreased by (protein) malnutrition and elevated by infectious disease.
Acute phase proteins (APP) are an ensemble of plasma proteins synthesized by the liver in response to tissue damage and inflammation associated with traumatic and/or infectious disease. Transferrin (Tf) and fibrinogen (Fb) are the most abundant acute proteins that can be accurately measured. There are additional proteins that become detectable when transferrin and fibrinogen levels are increased. Increased IgG and acute phase proteins indicate an infection with concurrent tissue damage. Increased IgG without increased fibrinogen indicates immunological response to infection without concomitant decrease in tissue function.
[IgG and APP are measured in 5 ul of serum using SDS-PAGE]
An example of SDS-PAGE of serum proteins from waved albatrosses (Phoebastria irrorata) Nazca boobies (Sula dactylatra) and common terns (Sterna hirundo). IgG concontration standards (2-10 ug) are used to construct a standard curve after densitometric scanning of the gel.
Arne Wilhelm Kaurin Tiselius was born August 10, 1902, in Stockholm. After the early loss of his father, the family moved to Gothenburg where he went to school, and after graduation at the local "Realgymnasium" in 1921, he studied at the University of Uppsala, specializing in chemistry. He became research assistant in The Svedberg's laboratory in 1925 and obtained his doctor's degree in 1930 on a thesis "The moving-boundary method of studying the electrophoresis of proteins" (published in Nova Acta Regiae Societatis Scientiarum Upsaliensis, Ser. IV, Vol. 7, No. 4) and was appointed Docent (Assistant Professor) in Chemistry from 1930 on. During the years 1931-1935 Tiselius published a number of papers on diffusion and adsorption phenomena in naturally occurring base-exchanging zeolites, and these studies were continued during a year's visit to H.S. Taylor's laboratory in Princeton with support of a Rockefeller Foundation Fellowship. Stimulated by many contacts with American biochemists and physical chemists during this visit, Tiselius on his return to Uppsala resumed his interest in proteins, and the application of physical methods to biochemical problems in general. This lead among other things to a much improved method of electrophoretic analysis, published in the Transactions of the Faraday Society, 33 (1937) 524. This method as applied to the study of serum proteins and to a number of other biochemical problems kept Tiselius and an increasing number of collaborators occupied for the following years. In 1938 a special research professorship was established for Tiselius through a donation to the University of Uppsala by Major Herbert Jacobsson and his wife. Some space was put at the disposal of the new professor in the Institute of Physical Chemistry (Prof. The Svedberg). In 1946 biochemistry was established as an independent department and in 1950-1952 obtained a new building, the present Institute of Biochemistry.
Under the leadership of Tiselius this institute has contributed to the development and improvement of a number of useful methods in biochemistry, such as electrophoresis, chromatography, phase partition, gel filtration, etc. These methods and others have been applied to studies of large molecular weight substances, chiefly proteins and enzymes, but also polysaccharides (dextran) and nucleic acids. There has always been a close contact between the methodological work and the research into special problems where the methods find their application. Tiselius took an active part in the reorganization of scientific research in Sweden in the years following World War II. Thus he was Chairman of the Swedish Natural Science Research Council 1946-1950, and Chairman of the Research Committee of the Swedish Cancer Society 1951-1955. He was President of the International Union of Pure and Applied Chemistry 1951-1955, became Vice President of the Nobel Foundation in 1947 and President since 1960. He has also served as member of the Nobel Committee for Chemistry since 1946.
He was married (1930) with Ingrid Margareta (Greta) Dalén, daughter of city judge Per Dalén of Gothenburg. They have two children: Eva (b. 1932), married to Dr. Torgny Bohlin, Lund; and Per (b. 1934), physician at the Academic Hospital, Uppsala.