Glutelins


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The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.

Glutelins

 

simple proteins present in the seeds of cereals and in the green parts of plants. Glutelins are soluble in weak alkaline solutions; they are not soluble in neutral aqueous and salt solutions or in alcohol. The study of glutelins is complicated by the fact that it is difficult to extract them in a pure form. Among the glutelins, glutenin from wheat and barley seeds, oryzenin from rice seeds, and glutelin from corn seeds have been well studied. Glutelins are reserve proteins; together with prolamins, they are found in the endosperm of seeds but not in the embryo. Glutelins are rich in glutanic acid and lysine.

The Great Soviet Encyclopedia, 3rd Edition (1970-1979). © 2010 The Gale Group, Inc. All rights reserved.
References in periodicals archive ?
Cooking may therefore promote physical and chemical changes in the proteins, particularly in glutelins, causing variations in the solubility of the proteins.
In raw grains, Fe is associated with albumins, prolamins, and glutelins, whereas in cooked grains Fe is linked to albumins and glutelins in most varieties.
Cooking results in a variation of the Fe concentration when associated with glutelins for the black, bolinha, rajado, and jalo beans, since it is possible to observe an increase (180%) and a decrease (78%) for the jalo and rajado beans, respectively.
Angiotensin I-converting enzyme-inhibitory activity was mainly found in glutelin (occurrence frequency 0.2045), followed by albumin (0.175) and three 7S globulins (0.1706) (Figure 2).
As shown previously, the most abundant fraction in nut was glutelin. A total of 21 peptides with different biological activities were found: (a) in the glutelin fraction, peptides with antihypertensive, antioxidant, and anticarcinogenic activities were detected.
It will be interesting in future studies to synthesize some of the peptides found in the glutelin and globulin fractions of nut (i.e., DMIPAQ, EEE, LKAWSVAR, VISR, LAASGLLLL, ALLALS, VDG, FQP, and CYFQNCPR) (Table 2) and test their potential to have an ACE inhibitory activity.
The glutelin fraction was less affected by heat stress.
The zein content was reduced by 61 and 45%, and the glutelin content was reduced by 36 and 33% of the control endosperms, in the growth chamber and field studies, respectively (Fig.
The albumin plus globulin and the glutelin fractions had the highest levels of radioactivity of all the protein fractions.
Structural relationship among the rice glutelin polypeptides.
Different solubility fractions of proteins (albumins, globulins, prolamins, and glutelins) were obtained as per Yamagata et al.
The prolamins and the glutelins, which are the two predominant groups of proteins in endosperm tissue (Muench and Okita, 1996), occurred at relatively low levels in embryos (Fig.