Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Fractionation of wheat gliadin and glutenin subunits by two-dimensional electrophoresis and the role of group 6 and group 2 chromosomes in gliadin synthesis (1981)
    Springer
    Theoretical and applied genetics 59 (1981), S. 349-359 
    Details
    ISSN: 1432-2242
    Keywords: Triticum aestivum ; Glutenin ; Gliadin ; Electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Subunits of wheat endosperm proteins have been fractionated by two-dimensional electrophoresis. To determine which subunits in the two-dimensional electrophoretic pattern belong to gliadin or glutenin the endosperm proteins have also been fractionated by a modified Osborne procedure and by gel filtration on Sephadex G-100 and Sepharose CL-4B prior to separation by two-dimensional electrophoresis. The control of production of five major grain protein subunits is shown to be determined by chromosomes 6A, 6B and 6D by comparing two-dimensional electrophoretic protein subunit patterns of aneuploid lines of the variety ‘Chinese Spring’. From these and previous studies it is concluded that some α, β and γ gliadins (molecular weights by SDS-PAGE 30,000 to 40,000) are specified by genes on the short arms of homoeologous Group 6 chromosomes, the ω gliadins (molecular weights by SDS-PAGE 50,000 to 70,000) are specified by genes on the short arms of homoeologous Group 1 chromosomes and the glutenin subunits (molecular weights by SDS-PAGE 〉 85,000) are specified by genes on the long arms of homoeologous Group 1 chromosomes. No major gliadins or glutenin subunits were absent when any of the chromosomes in homoeologous Groups 2, 3, 4, 5 or 7 were deleted. However two gliadins whose presumed structural genes are on chromosome 6D were absent in aneuploid stocks of ‘Chinese Spring’ carrying two additional doses of chromosome 2A. Two out of thirty-three intervarietal or interspecific chromosome substitution lines examined, involving homoeologous Group 2 chromosomes, lacked the same two gliadins. All the subunits in the other thirty-one chromosome substitution lines were indistinguishable from those in ‘Chinese Spring’. It is therefore concluded that the major variation affecting gliadin and glutenins in wheat is concentrated on the chromosomes of homoeologous Groups 1 and 6 but Group 2 chromosomes are candidates for further study. An endosperm protein controlled by chromosome 4D in ‘Chinese Spring’ is shown to be a high molecular weight globulin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276448
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...