Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
enabled [disable] Abstract
Number of results

Results found: 3

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
EN
Two-dimensional electrophoresis (2-DE) of soluble proteins and enzymes was performed and specific activities of 5 enzymes (esterase, pectinesterase, acid phosphatase, protease and diaphorase) were determined in stigmas of Lolium multiflorum (Italian ryegrass) treated with self or foreign pollen coat eluates (pc). Also, a low-molecular-weight fraction of the treated self-compatible (SC) and self-incompatible (SI) stigmas was analyzed by high-pressure liquid chromatography (HPLC). The treatment of stigmas with foreign pollen induced the loss of 42% of the control sample proteins in SC plants but only of 5.5% in SI plants. In contrast, the treatment of stigmas with foreign pollen induced the loss of 15% proteins in SC plants and of 29% in SI plants. Specific activities of esterase, pectinesterase and diaphorase were higher in SC than in SI stigmas. The 2-DE enzyme patterns indicated qualitative relationships between the presence of some isoforms of acid phosphatase or protease and the treatment with self or foreign pc in SC and SI stigmas. No changes were observed in HPLC profiles of the low-molecular-weight fraction from SC and SI stigmas treated or not with pc. The presented results revealed different reactions of SC and SI stigmas to the treatment with self or foreign pc. Further investigations may explain if any of the observed reactions represent specific reorientations in the style, facilitating cross- or self-pollination.
EN
Seven enzymatic systems in F1 Aegilops kotschyi and Ae. biuncialis ? Secale cereale hybrids, Aegilops kotschyi ? S. cereale amphiploids and their parental species (Ae. kotschyi, Ae. biuncialis and S. cereale) were analysed by starch and polyacrylamide gel electrophoresis. Five of them (phosphoglucose isomerase, glutamic oxalacetic transaminase, esterase, acid phosphatase, and diaphorase) were polymorphic and two (malic dehydrogenase and superoxide dismutase) were monomorphic. Several isophorms of phosphoclucose isomerase, esterase, acid phosphatase, and diaphorase were detected in some hybrids and amphiploids, but absent in the parents. The role of regulators, translocations and recombination is discussed in relation to the origin of these new isophorms. Some parental isozymes were absent both in hybrids and amphiploids, probably as a result of the suppression of structural genes in new combinations of the three genomes.
EN
Total proteins, esterases and acid phosphatases from pollen, seeds and leaves of three sunflower cultivars were separated by 2-D electrophoresis. The characteristic peptides for each cultivar were identified. The seeds and pollen of the cultivar Wielkopolski contained 45 and 37 characteristic peptides, respectively, while the seeds and pollen of Coril contained 73 and 35 characteristic peptides. The cultivar Frankasol had the lowest total number of stained peptides in seeds and pollen, and the number of the characteristic peptides was only 61 and 25, respectively. Analyses of esterases and acid phosphatases from young leaves and pollen led to identification of isoenzymes characteristic of the three cultivars. Only for Frankasol no specific acid phosphatase was observed, both in leaves and in pollen.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.