Allozyme variation within and among cultivated varieties of sweet chestnut (Castaneasativa)

1994 ◽  
Vol 24 (6) ◽  
pp. 1160-1165 ◽  
Author(s):  
S. Flneschi ◽  
M.E. Malvolti ◽  
M. Morgante ◽  
G.G. Vendramin
Keyword(s):  
Gel Electrophoresis ◽  
Southern Italy ◽  
Allozyme Variation ◽  
Starch Gel Electrophoresis ◽  
Enzyme Gene ◽  
Sweet Chestnut ◽  
Long Time ◽  
Starch Gel ◽  
High Degree ◽  
Southern European Countries

Sweet chestnut (Castaneasativa Mill.) is a species that has been cultivated and propagated through grafting for a long time in Italy and Southern European countries. The genetic variability within and among different varieties was analyzed by means of starch gel electrophoresis. Twenty cultivated varieties originating from three different areas located in northern, central, and southern Italy, were analyzed at six polymorphic enzyme gene loci. Our results show a relatively high degree of homogeneity both among individuals of the same variety and among varieties of the same area; on the other hand, high values of genetic distance were found among different geographic areas. The agamic propagation method of this species may have caused a reduction of the genetic diversity within varieties. The causes and consequences of the loss of genetic variation in these varieties are discussed.

Genetic diversity in red pine: evidence for low genic heterozygosity

1977 ◽  
Vol 7 (2) ◽  
pp. 343-347 ◽  
Author(s):  
D. P. Fowler ◽  
R. W. Morris
Keyword(s):  
Genetic Diversity ◽  
Gel Electrophoresis ◽  
Allozyme Variation ◽  
Red Pine ◽  
Starch Gel Electrophoresis ◽  
Banding Patterns ◽  
Coniferous Species ◽  
Low Degree ◽  
Starch Gel ◽  
Genetically Determined

Starch gel electrophoresis was used to survey for genetically determined enzyme mobility differences among 297 megagametophytes of red pine (Pinusresinosa Ait.) from five widely separated geographical sources. Consistent and reproducible enzyme banding patterns were observed with five of the seven isozyme systems assayed. No variation in band mobility was observed in any of these systems. This result stands in contrast with those reported from surveys of allozyme variation in other coniferous species but is consistent with the low degree of genetic variation observed in red pine for higher levels of genetic organization. It is concluded that red pine is genetically depauperate.Possible explanations for restricted genetic diversity are discussed. The most plausible explanation suggests that red pine was at sometime, possibly during the Pleistocene, reduced to a small refugial population and has yet to reestablish equilibrium heterozygosity.

Assessment of allozyme variation among New Zealand populations of Gracilaria chilensis (Gracialiares, Rhodophyta) using starch-gel electrophoresis

Hydrobiologia ◽  
1993 ◽  
Vol 260-261 (1) ◽  
pp. 159-165 ◽  
Author(s):  
Sompop Intasuwan ◽  
Margaret E. Gordon ◽  
Charles H. Daugherty ◽  
Graeme C. Lindsay
Keyword(s):  
New Zealand ◽  
Gel Electrophoresis ◽  
Allozyme Variation ◽  
Starch Gel Electrophoresis ◽  
Gracilaria Chilensis ◽  
Starch Gel

Little genetic variation in the oil sardine, Sardinella longiceps Val., from the western coast of India

1994 ◽  
Vol 45 (2) ◽  
pp. 257 ◽  
Author(s):  
MR Menezes
Keyword(s):  
Genetic Variation ◽  
Gel Electrophoresis ◽  
Western Coast ◽  
Starch Gel Electrophoresis ◽  
Marine Fish Species ◽  
Average Heterozygosity ◽  
Enzyme Gene ◽  
Starch Gel ◽  
Sardinella Longiceps ◽  
Gene Variability

Enzyme gene variability in the oil sardine, Sardinella longiceps, from three localities along the western coast of India was studied by starch-gel electrophoresis. Out of 19 loci scored, no locus was polymorphic by the 95% criterion. Seven loci were polymorphic at the P=0.99 level. The average heterozygosity ranged from 0.6% to 0.9%. These values are very low compared with those of other marine fish species.

Genetic and morphological variation among populations of Oxyna parietina (Diptera: Tephritidae) across a European transect

1992 ◽  
Vol 70 (6) ◽  
pp. 1120-1128 ◽  
Author(s):  
Sabine Eber ◽  
Roland Brandl ◽  
Stefan Vidal
Keyword(s):  
Gene Flow ◽  
Morphological Variation ◽  
Gel Electrophoresis ◽  
Regional Scale ◽  
Allozyme Variation ◽  
Starch Gel Electrophoresis ◽  
Allozyme Data ◽  
Starch Gel ◽  
Wing Morphometrics ◽  
Morphological Patterns

Genetic and morphological variation in the phytophagous tephritid Oxyna parietina (L.) was investigated across a transect through Central Europe by starch-gel electrophoresis to detect allozyme variation and by wing morphometrics. Very low allozyme differentiation was found on both a local and a regional scale, and is best explained by high rates and distances of gene flow. Nevertheless, there exists a smooth cline of allele frequencies from northern to southern populations. We tentatively interpret this cline as being a consequence of selection by environmental factors. The morphological patterns are not consistent with the allozyme data.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

STARCH GEL ELECTROPHORESIS OF MYOGEN FROM CHICKEN BREAST MUSCLE IN CONSTANT AND GRADIENT BUFFER SYSTEMS

1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Cacodylate ◽  
Gradient Systems ◽  
Optimal Separation ◽  
Starch Gel

By varying conditions of starch gel electrophoresis, factors contributing to the resolution of myogen proteins from chicken breast muscle have been studied. Variables examined included composition of the myogen extractant, protein concentration, ionic strength of electrophoretic media, pH of gel media, plane and direction of electrophoresis, and the nature of cations and anions in gel media and bridge solutions. The significance of anions was more closely studied with constant buffer systems, and gradient systems in which bridge electrolyte differed from, and gradually altered, the gel medium. Optimal separation was obtained in gradient systems with 0.10 M sodium chloride bridge solutions, and gel media of sodium cacodylate, pH 6.9, μ 0.010, which resolved 12 cationic zones, and sodium veronal, pH 7.4, μ 0.010, which resolved 10 anionic zones. These buffers in two-dimensional sequence revealed a total of about 24 components in this myogen.

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