Identity area
Type of entity
Authorized form of name
Parallel form(s) of name
Standardized form(s) of name according to other rules
Other form(s) of name
Identifiers for corporate bodies
Description area
Dates of existence
History
Ralph Ambrose Kekwick was born on 11 November 1908 at Woodford Wells in Essex. He was educated at the Leyton County High School for Boys and University College London, from where he graduated with First Class Honours B.Sc. in Chemistry in 1928. He remained at University College to undertake research, initially in physical chemistry under F.G. Donnan, then moving to study physical biochemistry under J.C. Drummond during which time he worked in close association with R.K. Cannan. In 1930 he was awarded a Bayliss-Sterling Memorial Scholarship and was also appointed Demonstrator in Biochemistry at University College. In 1931-1933 Kekwick held a Commonwealth Fund Fellowship. This enabled him to spend two years in the United States, studying with R.K. Cannan (who had by then moved to the New York University College of Medicine) and then researching problems of permeability at Princeton University and the Marine Biological Laboratories at Woods Hole, Massachusetts. Kekwick returned to the UK in 1933 to take up a post as Lecturer at University College London where he remained to 1937.
In 1935 Kekwick travelled to Sweden as a Rockefeller Foundation Fellow to work under T. Svedberg at the Institute of Physical Chemistry, University of Uppsala. This proved to be a key moment in Kekwick's career as he was introduced to the ultracentrifuge and electrophoresis apparatus, both developed at Uppsala. The ultracentrifuge, designed by Svedberg and colleagues, was used for the study of protein molecules in blood plasma. It separated out protein molecules to leave a pure protein preparation, for example plasma albumin and globulins while the rate of sedimentation could be measured to give a sedimentation co-efficient (a characteristic property of the protein). This allowed the molecular weight to be calculated and the proteins identified. The electrophoresis apparatus, designed by Tiselius, worked through the measurement of the negative electrical charge of proteins. As the size of the charge varies according to the protein's chemical structure, when an electrical charge was passed through a solution, proteins with a greater positive charge migrated towards the positive pole more rapidly. As with the ultracentrifuge this allowed the separation of different proteins in blood plasma and the diagnosis and monitoring of conditions in which the ratios of the blood plasma proteins were abnormal. These techniques contributed to general understanding of the part the proteins played in biological activity, the importance of fibrinogen in blood clotting, the role of gamma globulin in combatting infection and the role of albumin in maintaining the correct volume of blood. It also allowed for the diagnosis of medical conditions in which ratios of proteins in blood plasma were abnormal. Following this visit, in 1937 Kekwick was awarded a research grant from the Medical Research Council for electrophoretic and ultracentrifuge investigations on pathological and immune sera at the Lister Institute of Preventive Medicine. He was taken on the Scientific Staff of the Lister Institute in 1940.
During the Second World War Kekwick remained at the Lister Institute undertaking experimental and production work for the Medical Research Council's Blood Transfusion Research Committee. With A.S. McFarlane he devised a process to clarify outdated blood plasma so as to render it suitable for transfusion. He was appointed Head of the Lister's Biophysics Division in 1943 and he and his team worked on methods of freeze-drying plasma and then of separating out proteins in blood plasma. At the end of the war the MRC established a Blood Products Laboratory at the Lister Institute's station at Elstree, Hertfordshire. Kekwick worked closely with this Laboratory and was an adviser but continued his own research at the Lister Institute in Chelsea. He continued working on blood plasma analysis with ultracentrifuge and electrophoretic techniques and practical improvements in blood transfusion processes. In the 1950s he developed a method of fractionating out a fibrinogen fraction rich in Factor VIII, the anti-haemophilic globulin. This lead to the first clinical use of this Factor in 1957 and the establishment of a national laboratory dedicated to plasma fractionation. Kekwick's association with University College London continued. In 1954 he was appointed Reader in Chemical Biophysics and appointed to a personal Chair in Biophysics in 1966 (Emeritus and Fellow 1971). In addition to his pioneering work in blood plasma research, Kekwick contributed to developments in this area through his service on a number of Medical Research Council committees concerned with blood transfusion, haemophilia and hypogammaglobulinaemia. He served on the Committee of the British Biophysical Society 1967-1970. Kekwick was elected to the Fellowship of the Royal Society in 1966.