2006
DOI: 10.1007/bf02706623
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Is quantity of protein in barley forms determined by proteins localized in the subaleurone layer?

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Cited by 4 publications
(2 citation statements)
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“…A study from scanning electron microscopy and mass spectrometry suggests that the structure of the aleurone layer storing large quantities of protein did not differ between the high- and low-protein forms of barley biotypes. However, the quantity of protein in barley is determined by proteins localized in the sub-aleurone layer [69] . Two proteins, B3-hordein and Z-type serpin present in the sub-aleurone layer make the biggest quantitative difference between high- and low-protein kernels in forms of barley.…”
Section: Discussionmentioning
confidence: 99%
“…A study from scanning electron microscopy and mass spectrometry suggests that the structure of the aleurone layer storing large quantities of protein did not differ between the high- and low-protein forms of barley biotypes. However, the quantity of protein in barley is determined by proteins localized in the sub-aleurone layer [69] . Two proteins, B3-hordein and Z-type serpin present in the sub-aleurone layer make the biggest quantitative difference between high- and low-protein kernels in forms of barley.…”
Section: Discussionmentioning
confidence: 99%
“…The molecular masses of the obtained peptides were analysed using MALDI-TOF mass spectrometry. The results were analysed in silico using a procedure similar to that described previously (Ritte et al 2000;Macewicz et al 2006). A search of the accessible sequence databases resulted in sequence coverage at 31 %, and 33 out of 68 searched peptide masses matched StGWD3.…”
Section: In Situ Rt-pcrmentioning
confidence: 99%