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Journal ArticleDOI

Genetic control of multiple molecular forms of enzymes in plants: A review

John G. Scandalios
- 01 Feb 1969 - 
- Vol. 3, Iss: 1, pp 37-79
TLDR
The gel electrophoretic procedures have afforded the geneticist a means to study mutations which presumably alter the structure of enzymes, resulting in differential electrophoreic mobilities of the molecules, while their catalytic activity is retained.
Abstract
Progress in the field of biochemical genetics of diploid organisms has been considerable in the last decade. Much of this has been made possible by the introduction of improved electrophoretic procedures utilizing various gel matrices for separation of mixtures of proteins. Investigators of genetic control of protein synthesis have effectively used this tool to estimate the number of genes involved in the production of a protein or enzyme. These methods have already proved useful in providing information as to the number of polypeptide subunits that make up a protein molecule in studies with microorganisms (Levinthal et aL, 1962), animals (Markert, 1963), and plants (Scandalios, 1965a). In conjunction with the high-resolution \"zymogram\" method for displaying enzyme activity on gels (Hunter and Markert, 1957), the gel electrophoretic procedures have afforded the geneticist a means to study mutations which presumably alter the structure of enzymes, resulting in differential electrophoretic mobilities of the molecules, while their catalytic activity is retained. This is a new and promising dimension for studying gene action, since before the advent of these techniques similar studies were essentially confined to enzyme variation due to alterations in total catalytic activity. A large number of electrophoretic variants of enzymes have now been discovered (Shaw, 1965). With these findings came the knowledge that enzymes may exist in the same organism in more than one molecular form. Such multiple molecular forms of an enzyme in~ a single organism have been designated isozymes (Markert and Moller, 1959). Isozymes may differ in primary structure because they are encoded in different genes, either allelic or nonallelic. The primary structure may be further

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Journal ArticleDOI

Starch Gel Electrophoresis of Ferns: A Compilation of Grinding Buffers, Gel and Electrode Buffers, and Staining Schedules

TL;DR: An attempt to improve methods of analysis of fern enzymes in starch gel electrophoresis by experimenting with modifications of the method of sample preparation outlined by Soltis et al. (1980), and determining gel and electrode buffers that provide clear starch gel enzyme banding for 22 enzyme systems in ferns.
Journal ArticleDOI

Comparative Evolutionary Analysis of Chalcone Synthase and Alcohol Dehydrogenase Loci in Arabidopsis, Arabis, and Related Genera (Brassicaceae)

TL;DR: The authors analyzed sequence variation for chalcone synthase (Chs) and alcohol dehydrogenase (Adh) loci in 28 species in the genera Arabidopsis and Arabis and related taxa from tribe Arabideae.
Journal ArticleDOI

Electrophoretic Evidence and Plant Systematics

TL;DR: The advantages and limitations of electrophoretic evidence to test hypotheses in plant systematics and evolution and the results of a large number of studies which have utilized this evidence are discussed.
References
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Journal ArticleDOI

Multiple forms of enzymes: tissue, ontogenetic, and species specific patterns.

TL;DR: 2 Cleveland, L. R., J. R. R, and W. Nutting, J. L. Zool.
Journal ArticleDOI

Lactate Dehydrogenase Isozymes: Dissociation and Recombination of Subunits

TL;DR: Lactate dehydrogenase from beef tissues may be resolved electrophoretically into five isozymes each of which is a tetramer, which can be dissociated into monomers by freezing in 1M sodium chloride.
Journal ArticleDOI

Dissociation of lactate dehydrogenase into subunits with guanidine hydrochloride.

TL;DR: This report presents the results of treating lactate dehydrogenase with guanidine hydrochloride — a hydrogen bonding reagent which effectively ruptures the hydrogen bonds responsible for the secondary structure of many proteins.
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