Pseudocereals and Less Common Cereals 2002
DOI: 10.1007/978-3-662-09544-7_1
|View full text |Cite
|
Sign up to set email alerts
|

The Major Seed Storage Proteins of Spelt Wheat, Sorghum, Millets and Pseudocereals

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
24
0

Year Published

2006
2006
2023
2023

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 28 publications
(24 citation statements)
references
References 70 publications
0
24
0
Order By: Relevance
“…18 and 15 kD ( Figure 1B). The former are consistent with γ-zein and the latter with β-zein (Lawton and Wilson, 2003) and possibly also the 16 kDa γ-zein (Shewry, 2002). Thus, the 2-D PAGE showed that the total zein comprised the all the major zein sub-classes, α-, β-, γ-and δ-zein which are present in maize kernels, and that the commercial zein was predominantly α-zein.…”
Section: -D Pagementioning
confidence: 77%
“…18 and 15 kD ( Figure 1B). The former are consistent with γ-zein and the latter with β-zein (Lawton and Wilson, 2003) and possibly also the 16 kDa γ-zein (Shewry, 2002). Thus, the 2-D PAGE showed that the total zein comprised the all the major zein sub-classes, α-, β-, γ-and δ-zein which are present in maize kernels, and that the commercial zein was predominantly α-zein.…”
Section: -D Pagementioning
confidence: 77%
“…Research and development on acha and iburu cereal grains is experiencing renewed interest in Africa and the rest of the world, particularly for its flavour and nutritional qualities (Jideani et al 2000;Shewry 2002;Koreissi et al 2007). Acha and iburu proteins have composition similar to that of white rice (Temple and Bassa 1991;Jideani and Akingbala 1993), but having relatively higher sulphur amino acid (methionine and cystine) content (de Lumen et al 1993;Lasekan 1994;Jideani et al 1994a).…”
Section: Uniqueness Of Acha and Iburu Cereal Grain Proteinsmentioning
confidence: 98%
“…Zein, kafirin and pennisetin prolamins, presumably as a result of their relative hydrophobicity and disulphide bond cross-linking (Shewry, 2002;Belton et al, 2006), are isolated in protein bodies in the starchy endosperm cells of the mature grain (Adams et al, 1976). Likewise, the rice prolamins are isolated in Type I protein bodies (Saito et al, 2012) and the glutelins are isolated in Type II protein bodies (Yamagata et al, 1982) and in oats the globulin and prolamin storage proteins are co-located in the same protein bodies (reviewed by .…”
Section: Isolation In Protein Bodiesmentioning
confidence: 99%