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  • 1980-1984  (6)
  • Phaseolus vulgaris  (5)
  • Benign prostatic hyperplasia  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Interaction of prolactin and testosterone in the human prostate (1981)
    Springer
    Urological research 9 (1981), S. 79-88 
    Details
    ISSN: 1434-0879
    Keywords: Prolactin ; Prostate cancer ; Benign prostatic hyperplasia ; Androgen metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Three experiments were performed to determine whether human prolactin (hPr) affects prostatic uptake and metabolism of testosterone (T). 1) Patients with prostatic cancer were infused twice with radio-labelled androgens, the first time with basal hPr, the second time with oral thyrotrophin-releasing hormone (TRH)-elevated hPr. In 5/7, significant increases in metabolic clearance of dihydrotestosterone (DHT) and in conversion of T to DHT accompanied increased hPr. 2) The incorporation of labelled T into minced benign prostatic hypertrophy (BPH) tissue from subjects with high (40 ng/ml) hPr was measured and was found to be more than twice the uptake into tissue from those with low hPr (6.5±1.9 ng/ml). 3) Uptake and metabolism in vivo of a bolus of 3H-T by BPH and carcinomatous prostates was measured and was far greater in subjects whose hPr was elevated by chlorpromazine than in untreated controls. It is concluded that prolactin increases prostatic uptake and metabolism of T. It is suggested that the best management of prostatic cancer should include depletion of prolactin as well as androgen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00256681
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    Paper (German National Licenses)
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  • 2
    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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    Paper (German National Licenses)
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  • 3
    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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    Paper (German National Licenses)
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  • 4
    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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    Paper (German National Licenses)
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  • 5
    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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    Paper (German National Licenses)
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  • 6
    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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    Paper (German National Licenses)
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