An electrophoretic survey of seedling isozymes in several Phaseolus species

Abstract

INDEX WORDSEsterase, acid phosphatase, peroxidase, banding pattern, tissue specificity, species relationships. SUMMARYStarch-gel electrophoresis was used to study esterase, acid phosphatase, and peroxidase isozyme patterns in the primary leaves, stems, and roots of 13 species within the genus Phaseolus (P. acutifolius, P. adenanthus, P. angularis, P. atropurpureus, P. aureus, P. bracteatus, P. calcaratus, P. lathyroides, P. mungo, P. ricciardianus, domestic P. vulgaris, and wild P. coccineus and P. vulgaris). Most species showed unique banding patterns in each isozyme system. However, a close similarity in banding patterns was observed for the domestic P. vulgaris, wild P. vulgaris, and wild P. coccinkus indicating close genetic relationships, possibly through species introgression or common descent.Great differences in isozyme patterns were found for different tissues from the same species in all systems indicating the high tissue specificity of isozymes. Upon compilation of bands from all the species, a very large number of isozymes were obtained in each system or tissue, making the electrophoretic isozyme technique of high potential in studies of isozyme variants in this genus.

Isoenzymatic variability in wild potatoes

“…There were three to eight bands per pattern (Figure 2). According to Bassiri & Adams (1978), systems with higher number of polymorphic bands, such as peroxidase, are the most adequate to identify cultivars. These enzymes (group II) act over a class of molecules which, normally, come from the environment and that can have qualitatively and quantitatively more variables than enzymes (group I) which act on in vivo substrates, generally restricted to molecules that are products of a previous internal enzymatic reaction (Kojima et al, 1970).…”

Extensive introgression of Middle American germplasm into Chilean common bean cultivars

“…Isozyme variation in Phaseolus has been used to confirm the hypothesis of multiple domestication of common bean (Sprecher, 1988;Koenig & Gepts, 1989b;Singh et al, 1991c), to evaluate multilocus associations (Gepts, 1989), measure differential elimination of donor parents in crosses (Wall, 1968), measure genetic diversity between genotypes (West & Garber, 1967;Wall & Wall, 1975;Bassiri & Adams, 1978a, 1978bWeeden, 1984b;Sprecher, 1988;Koenig & Gepts, 1989b;Singh et al, 1991c), and identify the organization of common bean gene pool into different races (Singh et al, 1991a).…”

Genetic Diversity of Bulgarian Phaseolus vulgaris L. Germplasm Collection Through Phaseolin and Isozyme Markers

“…West & Garber (1967) and Bassiri & Adams (1978) proved the existence of a close similarity between P. vulgaris and P. coccineus as well as the possibility to develop hybrids of these two species. Despite their cross-ability, there is a problem with rejecting the genome that originates from the male gametophyte (Wall, 1968;Wall & Wall, 1975;Guo et al, 1989).…”

“…Lefort-Buson et al (1985), Roux (1987) and summarize the different uses of isozymes in breeding. The enzymatic analysis has allowed the identification of certain species of the Phaseolus-Vigna complex to be improved (West et al, 1967a;Bassiri et al, 1978a;Jaaska & Jaaska, 1988), and the study of the species P. coccineus (West & Gabet, 1967b;Bassiri et al, 1978;Pinero et al, 1988). Despite the possibility of a crossover between these two species, there is rejection of the genome of the male gametophyte (Wall, 1968;Wall et al, 1975;Guo et al, 1989).…”

“…The organ used is young, since the enzymatic activity is at its peak. The preparation of gels, electrophoresis buffers, the loading of samples and the conditions for separation were developed by Bushuk et al (1978), Bassiri et al (1978), Aebersold et al (1987), Pasteur et al (1987), Stuber et al (1988), Charlionet (1990), Hames (1990), , ), Acquat (1993. To make an enzyme visible, the gel is immersed in a liquid reaction medium with a specific substrate for the enzyme system studied and various chemical compounds whose activity is needed (a coenzyme, ion, etc.).…”