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  • 1
    Electronic Resource
    Electronic Resource
    Genetic variation in the subunits of globulin-1 storage protein of French bean (1981)
    Springer
    Theoretical and applied genetics 59 (1981), S. 83-88 
    Details
    ISSN: 1432-2242
    Keywords: Phaseolus vulgaris ; Storage proteins ; Electrophoresis ; Genetic variation ; Banding types
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Charge and molecular weight heterogeneity of globulin-1 (G1) polypeptides of the bean, Phaseolus vulgaris L., were revealed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Different bean cultivars were classified into three groups: ‘Tendergreen’, ‘Sanilac’, and ‘Contender’ on the basis of their protein subunit composition. Nine distinct major bands: α51,α49, α48.5,β48T, β48S, β47, γ45.5, γ45S, and γ45C, and two minor bands: γ46T and γ46S were found to account for the three profiles seen on one-dimensional SDS-PAGE. Two-dimensional analysis revealed these eleven protein bands to be composed of a minimum of fourteen distinct protein subunits. The ‘Tendergreen’ and ‘Sanilac’ types differ in their G1 polypeptide composition. The protein patterns of the ‘Contender’ types are intermediate, containing many protein subunits found in the patterns of the ‘Tendergreen’ and ‘Sanilac’ types suggesting a genetic and evolutionary relationship.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00285895
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  • 2
    Electronic Resource
    Electronic Resource
    Linkage relationships between genes controlling seed proteins in French bean (1981)
    Springer
    Theoretical and applied genetics 60 (1981), S. 251-259 
    Details
    ISSN: 1432-2242
    Keywords: Phaseolus vulgaris ; Phaseolin ; Seed proteins ; Electrophoresis ; Linkage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The inheritance of phaseolin and globulin-2 (G2)/albumin polypeptides was investigated in crosses involving varieties which exhibited the three electrophoretic banding patterns of phaseolin found in French bean. ‘Total’ seed protein extracts of single seeds of the F1 and F2 generations from the crosses: ‘Sanilac’ × ‘Contender’, ‘BBL 240’ × ‘Contender’, and ‘Sanilac’ × ‘BBL 240’ were analyzed by two-dimensional electrophoresis. Segregation of the genes controlling phaseolin and G2/albumin polypeptides, and those controlling a further five groups of seed proteins (A, B, D, E, and F) were observed. No recombinant electrophoretic phenotypes were seen for phaseolin or G2/albumin polypeptides suggesting that the genes controlling each of these groups of polypeptides are closely linked and segregate like single Mendelian genes. The phaseolin genes and G2/albumin genes were not linked to each other. The group of genes controlling phaseolin polypeptides were linked to those controlling group B proteins, and those controlling G2/albumin polypeptides were linked to those controlling group F proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02342545
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  • 3
    Electronic Resource
    Electronic Resource
    Bean lectins (1982)
    Springer
    Theoretical and applied genetics 62 (1982), S. 263-271 
    Details
    ISSN: 1432-2242
    Keywords: Phaseolus vulgaris ; Seed protein ; Lectins ; Electrophoresis ; Agglutination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Single seeds of over 100 bean cultivars were analyzed by two-dimensional electrophoresis. The cultivars could be classified into eight groups by virtue of their G2/albumin electrophoretic patterns: TG2, SG2, VG2, PrG2, BG2, MG2, PG2, and PiG2, The polypeptide compositions of these types were largely inter-related having particular polypeptides in common. It was possible to correlate the G2/albumin patterns with agglutinating activity of cow and rabbit blood cells as measured by the agglutination ratio (minimum concentration of extract required to agglutinate cow blood cells: minimum concentration of extract required to agglutinate rabbit blood cells). The active lectin polypeptides were identified by extracting lectins from agglutinated erythrocytes and by comparing the qualitative similarities and differences of the G2/albumin patterns and their agglutination activities. A reference catalogue of over 100 bean cultivars giving their phaseolin and G2/albumin electrophoretic patterns, and agglutination ratios is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276249
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  • 4
    Electronic Resource
    Electronic Resource
    Bean lectins (1982)
    Springer
    Theoretical and applied genetics 62 (1982), S. 361-367 
    Details
    ISSN: 1432-2242
    Keywords: Phaseolus vulgaris ; Lectins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The relationship between the polypeptide composition and the agglutination behaviour of the lectin-containing G2/albumin protein groups has allowed the identification of the active lectin polypeptides in different cultivars of Phaseolus vulgaris (Brown et al. accompanying paper). These results were used to ascertain the particular G2/albumin group contained in the various lectin sources used previously for the purification of lectin proteins. Many studies were found to have included lectin sources which contained the same G2/albumin pattern (TG2) and this common denominator has permitted the direct comparison of the properties reported for these purified lectins. Thus, much of the extensive literature on bean lectins is concurred.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00275105
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  • 5
    Electronic Resource
    Electronic Resource
    Bean lectins (1985)
    Springer
    Theoretical and applied genetics 70 (1985), S. 22-31 
    Details
    ISSN: 1432-2242
    Keywords: Phaseolus vulgaris ; Lectin ; Phaseolin ; Quantitative variation ; Immunoelectrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Seeds of forty bean cultivars having different lectin types based on two-dimensional isoelectric focusing-sodium dodecyl sulfate polyacrylamide gel electrophoresis (IEF-SDS/PAGE) were analyzed for quantities of lectin, phaseolin and total protein. Significant differences were found among groups of cultivars with different lectin types for the quantity of lectin and phaseolin. Cultivars with more complex lectin types based on IEF-SDS/PAGE tended to have higher quantities of lectin and lower quantities of phaseolin than cultivars with simple lectin types. An association between lectin type and the quantity of lectin and phaseolin was found also in the seeds of F2 plants that segregated in a Mendelian fashion for two lectin types. Seeds from plants with the complex lectin type had more lectin and less phaseolin than seeds from plants with the simple lectin type. Therefore, the genes controlling qualitative lectin variation also may influence the quantitative variation of lectin and phaseolin. The results of this study are related to other studies on the quantitative variation for seed proteins and to the possible molecular basis for variation in the quantity of lectins in beans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264478
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  • 6
    Electronic Resource
    Electronic Resource
    Bean lectins IV: genetic variation in the non-denatured structure of lectins from different Phaseolus vulgaris L. cultivars (1984)
    Springer
    Theoretical and applied genetics 67 (1984), S. 547-552 
    Details
    ISSN: 1432-2242
    Keywords: Phaseolus vulgaris ; Lectins ; Albumin ; Globulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Variation in the native conformation of bean lectins was examined using electrophoresis of non-denatured total protein extracts and purified albumin and globulin lectin. The observed variation was related to the genetic variation reported previously for lectin polypeptide composition as revealed by two-dimensional isoelectricfocusing-sodium dodecyl sulfate polyacrylamide gel electrophoresis (IEF-SDS/PAGE). When eleven cultivars with different IEF-SDS/PAGE lectin polypeptide compositions were compared, eight had unique non-denatured lectin patterns and three had identical patterns. For some cultivars differences in non-denatured lectin patterns were observed between the purified albumin and globulin lectin preparations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264902
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  • 7
    Electronic Resource
    Electronic Resource
    Angiotensin II binding to tissues of the rainbow trout, Oncorhynchus mykiss, studied by autoradiography (1992)
    Springer
    Journal of comparative physiology 162 (1992), S. 197-202 
    Details
    ISSN: 1432-136X
    Keywords: Angiotensin II ; Autoradiography ; Seawater-adaptation ; trout, Oncorhynchus mykiss (= Salmogairdneri)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Tissue slices from seawater-adapted and freshwater-adapted rainbow trout, Oncorhynchus mykiss, were exposed to 125I-angiotensin II (1.01·10-9 M) and binding sites located by light-microscopic autoradiography. Binding/uptake was significantly inhibited by excess (10-5 M) unlabelled angiotensin II, suggesting specific binding/uptake of angiotensin II to the ventral and dorsal aorta (smooth muscle), urinary bladder (smooth muscle and epithelial lining), glomeruli and proximal tubules, the gill (lamellae and central filament), skin (epithelium), intestine and oesophagus (mucosal epithelium), liver, heart (ventricular myocytes), adrenocortical tissue and brain (cerebellum and medulla oblongata). The specific binding/uptake of angiotensin II to tissues of freshwater- and seawater-adapted animals were generally similar. However, binding/uptake by the proximal tubules was significantly higher in freshwater-adapted trout than seawater-adapted trout. Specific binding/uptake of angiotensin II by the smooth muscle of the bladder was significantly higher in trout adapted to seawater than trout adapted to freshwater.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00357523
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  • 8
    Electronic Resource
    Electronic Resource
    Direct effects of angiotensin II on glomerular ultrastructure in the rainbow trout, Salmo gairdneri (1990)
    Springer
    Cell & tissue research 260 (1990), S. 315-319 
    Details
    ISSN: 1432-0878
    Keywords: Glomerulus ; Angiotensin II ; Glomerular ultrastructure ; Seawater adaptation ; Salmo gairdneri (Teleostei)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Slices from the kidneys of the rainbow trout which were exposed to 10-6 or 10-5 M angiotensin II (AII) and isolated glomeruli exposed to 10-7 or 10-5 M AII showed ultrastructural changes compared to control tissues incubated without AII. The studies indicate that angiotensin II has a direct action on glomerular ultrastructure, flattening the epithelial podocytes and broadening the primary processes with fusion of pedicels in extreme cases. These changes suggest a probable effect of AII on water permeability of the trout glomerulus, an intrarenal action which is believed to form an essential part of the antidiuretic adaptation to increased environmental salinities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318634
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  • 9
    Electronic Resource
    Electronic Resource
    Glomerular ultrastructure of the trout, Salmo gairdneri: Effects of angiotensin II and adaptation to seawater (1987)
    Springer
    Cell & tissue research 249 (1987), S. 437-442 
    Details
    ISSN: 1432-0878
    Keywords: Angiotensin II ; Glomerulus ; Salmo gairdneri ; Seawater-adaptation ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The effect of angiotensin infusion on the glomerular ultrastructure of freshwater- and seawater-adapted rainbow trout, Salmo gairdneri, has been examined by scanning and transmission electron microscopy. Adaptation of trout to seawater resulted in epithelial podocyte flattening, primary process broadening and apparent loss of foot processes in almost all glomeruli, features which were uncommon in freshwater-adapted trout. Similar changes were induced by infusion of freshwater-adapted animals with angiotensin, suggesting that the renin-angiotensin system plays a role in the modification of glomerular epithelial ultrastructure. Adaptation of trout to seawater also reduced glomerular diameter, but infusion of freshwater-adapted animals with angiotensin did not mirror this effect. Infusion of angiotensin into seawater-adapted animals increased the overall thickness of glomerular basement membrane by increasing the lamina rara interna and lamina densa. This did not occur when freshwater-adapted fish were either infused with angiotensin or adapted to seawater. These findings suggest that other humoral systems are involved in the control of glomerular diameter and basement membrane thickness as part of an integrated response to increased environmental salinity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00215528
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  • 10
    Electronic Resource
    Electronic Resource
    Glomerular binding of angiotensin II in the rainbow trout,Salmo gairdneri (1990)
    Springer
    Cell & tissue research 259 (1990), S. 479-482 
    Details
    ISSN: 1432-0878
    Keywords: Kidney ; Glomerulus ; Angiotensin II ; Salmo gairdneri (Teleostei)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Isolated glomeruli of the rainbow trout have been exposed in vitro to125I-angiotensin II (0.88 × 10−9 M) and binding sites located by light-microscopic autoradiography. These studies provide evidence of specific binding of angiotensin II by glomeruli. Binding was significantly inhibited by excess (10−5 M) unlabelled angiotensin II, but a high degree of non-specific binding also occurred. The mammalian competitive antagonist, saralasin (3 × 10−7 M) did not influence125I-angiotensin II binding to fish glomeruli. Intense binding of125I-angiotensin II was noted at the vascular pole of some glomeruli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01740774
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