scholarly journals Gordon Henry Dixon. 25 March 1930 — 24 July 2016

Author(s):  
Rafael Oliva ◽  
Stephen A. Krawetz ◽  
GHD Consortium

Gordon H. Dixon was a highly influential scientist who excelled in all the stages of his career and in each laboratory of every institution at which he was a member. Gordon began his graduate career at the University of Cambridge and completed his studies at the University of Toronto on the subject of transpeptidation reactions in biological systems. At an early stage of his career, he developed the technique of starch gel electrophoresis with Oliver Smithies and made important discoveries on the structure of human haptoglobins. Subsequently, Gordon contributed to the determination of the structure and active sites and mechanisms of action of trypsin and chymotrypsin and made seminal discoveries related to understanding the structure of the protein hormone insulin. However, he is best known for his later studies on the regulation of protamine genes and chromatin transitions in spermatogenesis. He is often considered to be the father of the protamine molecular biology underlying this gene system and his research is continually cited to this day. Gordon contributed to the identification and sequencing of the protamine genes, the discovery that methionine was required for initiation of protamine synthesis, understanding the roles of histone hyperacetylation and protamine phosphorylation, and the generation of the highly compact nucleoprotamine structure present in sperm, primarily using trout as a model system. Gordon is fondly remembered as a brilliant and very generous scientist by all his mentees, representing all levels from undergraduates to PhD and postdoctoral fellows, who provided a scientifically stimulating atmosphere in which they could develop their careers. From a more personal perspective, he also had a fun side and was devoted to his family. Gordon was a person who, owing to his legacy of great science and his fundamental humanity, still lives in the memory of many people.

1960 ◽  
Vol 6 (3) ◽  
pp. 254-262 ◽  
Author(s):  
C A J. Goldberg ◽  
A C Ross

Abstract It has been shown that variations in the preparation of the starch gel and in photographic interpretation can significantly affect the accuracy of the measurement of hemoglobin A2. An improved method for the determination of hemoglobin A2 by starch-gel electrophoresis has been presented which affords greater accuracy than was previously achieved. Hemoglobin A2 concentrations for healthy persons and patients with sickle cell trait, various nonthalassemic anemias, and thalassemia trait have been presented.


1958 ◽  
Vol 4 (6) ◽  
pp. 484-495 ◽  
Author(s):  
C A J Goldberg

Abstract A method for starch gel electrophoresis of hemoglobins is presented in which a modified Lintner starch is used for the preparation of the gel. A discontinuous buffer system of tris-EDTA-borate/barbital is used as the electrolyte medium because of its superior resolving power. Hemoglobin A2 values, obtained with this method, of healthy individuals, patients with thalassemia, and those with various anemias of nonthalassemic origin are presented.


1966 ◽  
Vol 14 (1) ◽  
pp. 25-32 ◽  
Author(s):  
FRANK H. RUDDLE

The water soluble esterases extracted from the kidney tissue of three inbred mouse strains (C57BL/6J, RF/J and SJL/J) are described. The analysis of the esterases was performed by means of starch gel electrophoresis. Between 25 and 30 esterase active sites (bands) were identified. A description and a classification are given for these esterases. Classification is based on relative electrophoretic mobilities and pharmacological properties of the esterases. Esterase polymorphisms are described between the three inbred strains studied. Esterase sexumal dimorphisms are also reported for these strains. Finally, information is given regarding the contribution ( i.e., contamination) of serum esterases to the kidney esterase patterns.


1967 ◽  
Vol 105 (2) ◽  
pp. 599-604 ◽  
Author(s):  
A. E. H. Emery

1. A technique has been developed, based on preferential inhibition by urea, for determining the amounts and proportions of the M and H sub-units of lactate dehydrogenase (referred to as LDH-M and LDH-H respectively) in human tissues, including muscle. 2. There was good agreement between the results obtained with urea inhibition and those obtained with starch-gel electrophoresis. 3. With increasing age there was a significant decrease in the total amount of lactate dehydrogenase and the amount of LDH-M in skeletal muscle. This could not be accounted for by the replacement of functioning muscle tissue by fibrous connective tissue. 4. The proportion of LDH-M was less in certain muscles (e.g. soleus and extra-ocular) than in other muscles (e.g. gastrocnemius and rectus abdominis). 5. The proportions of LDH-M and LDH-H did not differ significantly in different superficial limb muscles and were not significantly affected by either age or sex. 6. Specimens of muscle from 86 different individuals (all Europeans) have been subjected to electrophoresis, but no variants of lactate dehydrogenase isoenzymes have been found.


2015 ◽  
Vol 33 (2) ◽  
pp. 7-17
Author(s):  
Carl Morey

In this article the author reflects on musical life in Canada, drawing on experiential perspectives while growing up in Toronto and his career for three decades as a faculty member in musicology at the Faculty of Music at the University of Toronto. References to pivotal musical institutions (Canadian League of Composers, CBC, Canadian Music Centre, among others) and historical documents such as Ernest MacMillan’sMusic in Canada,Marshall McLuhan’sGutenberg Galaxy,and George Grant’sLament for a Nationprovide contextual frameworks for these perspectives.


2003 ◽  
Vol 81 (1-2) ◽  
pp. 145-157
Author(s):  
M J Clouter

Harry Kiefte (1942–1997) was born in Amsterdam and moved to Toronto at an early age where he completed his formal education. His Ph.D. research was in the field of electron paramagnetic resonance under J.S.M. Harvey at the University of Toronto. He then completed two years of postdoctoral study with B.P. Stoicheff at the same institution where he participated in the pioneering work that led to the recording of the first Brillouin spectra from single crystals of rare-gas solids and the consequent determination of the elastic constants for these materials. It was the technique of Brillouin spectroscopy, and its application to the determination of the elastic properties of a wide range of crystalline materials, that engaged his interest and very considerable talents for the remainder of his career at the Department of Physics, Memorial University, where he accepted a faculty position in 1973. At the time of his death, at the relatively young age of 54, his name appeared as author or co-author on approximately 90 publications. Included among the co-authors were four graduate students whose research was devoted to ice-related studies. It is this significant contribution to our knowledge of the elastic properties of ice that will be reviewed in this paper. PACS No.: 62.20Dc


1965 ◽  
Vol 32 (2) ◽  
pp. 181-186 ◽  
Author(s):  
H. A. Veringa ◽  
M. F. Kerkhof Mogot

SummaryWhole casein, β-casein, β-lactoglobulin and euglobulin were labelled with 131I. The conditions under which iodination was carried out were chosen so as to avoid any modification of the original characteristics of the proteins. This was checked by starch-gel electrophoresis and determination of sedimentation constants, apparent molecular weights and, for euglobulin, the clustering effect on fat globules.As was shown by autoradiograms of the starch-gel plates, the radioactivity was incorporated in all zones of the electrophoresis pattern.


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