Protein distribution pattern in floury and vitreous endosperm of maize grain
Alpha-amino nitrogen compounds of floury and vitreous parts of hand-dissected endosperm from eight maize (Zea mays L.) inbred lines, representing a broad range of vitreousness (42-95%), were isolated as nonprotein nitrogen, albumin-globulins, zeins, and true glutelins. The three protein classes aver...
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Published in: | Cereal chemistry Vol. 81; no. 2; pp. 153 - 158 |
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Main Authors: | , , |
Format: | Journal Article |
Language: | English |
Published: |
St. Paul, MN
The American Association of Cereal Chemists, Inc
01-03-2004
American Association of Cereal Chemists |
Subjects: | |
Online Access: | Get full text |
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Summary: | Alpha-amino nitrogen compounds of floury and vitreous parts of hand-dissected endosperm from eight maize (Zea mays L.) inbred lines, representing a broad range of vitreousness (42-95%), were isolated as nonprotein nitrogen, albumin-globulins, zeins, and true glutelins. The three protein classes averaged, respectively, 13, 48, and 35% of total nitrogen in floury endosperm, and 4, 79, and 15% of that in vitreous endosperm. For six inbreds, floury endosperm was richer in 27 kDa gamma-zein than vitreous endosperm; the reverse was found for an Argentine flint inbred (ARGL 256), and only traces of 27 kDa gamma-zein occurred in both floury and vitreous endosperm of inbred F113. Results were compared with protein distribution patterns reported in the literature of whole endosperm of wild-type and mutant genotypes of maize, and with wild relatives of maize, Tripsacum, and teosintes. When percentage of salt-soluble nitrogen increased from 2% (Tripsacum) to 22% (in double mutant Oh43o2;bt2), zeins decreased from 87 to 22%, and true glutelins increased from 11 to 57%. The pattern of whole endosperm of Zea perennis was very similar to that of the vitreous endosperm of line ARGL 256. The mean pattern for whole endosperm of six o2 inbred lines was identical to that of floury endosperm of eight wild-type lines, consistent with a lack of synthesis of alpha-zeins due to the mutation in the O2 gene. |
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ISSN: | 0009-0352 1943-3638 |
DOI: | 10.1094/cchem.2004.81.2.153 |