Library

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
    s.l. : American Chemical Society
    Biochemistry 21 (1982), S. 4843-4849 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 28 (1980), S. 904-908 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 93 (1995), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A cathepsin D-like aspartic proteinase (EC 3.4.23) is abundant in ungerminated barley (Hordeum vulgare) seed while a 30 kDa cysteine endoproteinase (EC 3.4.22) is one of the proteinases synthesized de novo in the germinating seed. In this work, the localization of these two acid proteinases was studied at both the tissue and subcellular levels by immunomicroscopy. The results confirm that they have completely different functions. The aspartic proteinase was present in the ungerminated seed and, during germination, it appeared in all the living tissues of the grain, including the shoot and root. Contrary to previous suggestions, it was not observed in the starchy endosperm. By immunoblotting, the high molecular mass form of the enzyme (32 + 16 kDa) was found in all the living tissues, whereas the low molecular mass form (29 + 11 kDa) was not present in the shoot or root, indicating that the two enzyme forms have different physiological roles. The aspartic proteinase was localized first in the scutellar protein bodies of germinating seed, and later in the vacuoles which are formed by fusion of the protein bodies. In contrast to the aspartic proteinase, the expression of the 30 kDa cysteine proteinase began during the first germination day, and it was secreted into the starchy endosperm; first from the scutellum and later from the aleurone layer. It was not found in either shoots or roots. The 30 kDa cysteine proteinase was detected in the Golgi apparatus and in the putative secretory vesicles of the scutellar epithelium. These results suggest that the aspartic proteinase functions only in the living tissues of the grain, as opposed to the 30 kDa cysteine proteinase which is apparently one of the proteases initiating the hydrolysis of storage proteins in the starchy endosperm.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1572-9788
    Keywords: lodging ; marker assisted selection ; near isogenic lines ; plant height ; QTL
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Three previously identified grain yield quantitative trait loci (QTL) on chromosomes 2S(2HS), 3C(3HC) and 5L(1HL), designated QTL-2S, QTL-3 and QTL-5L, respectively, were evaluated for their potential to increase yields of high-quality malting barley without disturbing their favorable malting quality profile. QTL mapping of yield related traits was performed and near-isogenic lines (NILs) were developed. QTL for plant height, head shattering, seed weight and number of rachis nodes/spike were detected in the QTL-3 region. NILs developed by introgressing QTL-3 from the high-yielding cv. Steptoe to the superior malting quality, moderate-yielding cv. Morex acquired reduced height, lodging and head shattering features of Steptoe without major changes in malting quality. The yield of NILs, measured by minimizing the losses due to lodging and head shattering, did not exceed that of Morex. Steptoe NILs, with the Morex QTL-2S region, flowered 10 days later than Steptoe but the grain yield was not changed. None of the 3 QTL studied altered the measured yield of the recipient genotype, per se, although QTL 2S and QTL-3 affected yield-related traits. We conclude that these yield QTL must interact with other genes for full expression. Alternatively, they affect the harvestable yield through reduced lodging, head shattering, and/or altered flowering time.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...