zein/zea mays

A zein-degrading protease (ZDP) from Zea mays was heterologously expressed using Pichia pastoris and its characteristics and effects on enzymatic hydrolysis of corn starch were investigated in the current study. The optimal temperature and pH for ZDP activity was 40 °C and pH 5.0, respectively. The

We studied three mutations, opaque-2 (o2), opaque-7 (o7), and floury-2(fI2), each of which causes a depression in zein synthesis. We examined the processing efficiencies of the rough endoplasmic reticulum membranes in vitro, the levels of RNA transcription using cloned zein probes, and the genomic

Zeins constitute 60-70% of maize endosperm protein. Zein genes are specifically transcribed in the endosperm, and a correlation has been established between tissue-specific expression and demethylation. Three inbred lines and their reciprocal crosses were analysed to assess for allele-specific

Zein messenger RNAs from maize endosperm were purified by successive oligo(dT)-cellulose chromatography and sucrose gradient centrifugation. Polyacrylamide gel electrophoresis under denaturing conditions revealed the presence of two size classes of zein messenger RNAs of Mr 3.5 x 10(5) and 4.10 x

Mature endosperms from opaque-2 mutant seeds with various genetic backgrounds (B 37, W 64A, R 802A and Oh 43) contained twice as much globulin than the corresponding normals, reduced amounts of zein and an increased amount of albumin. The latter is caused by a diminished disappearance of albumins in

Genetic control of the major zein polypeptides in maize (Zea mays L.) was studied by isoelectric focusing (IEF) in agarose. Linkage relationships were determined by making a number of crosses, then determining the expression of zein polypeptides in backcross seeds. Chromosome linkages were

Continuous cultures, established 10 days after pollination from endosperms of inbred A636 Zea mays (L.) were extracted 21 months later with aqueous ethanol. The solubilized proteins were analyzed by poly-acrylamide-sodium dodecyl sulfate gel electrophoresis. Two protein bands co-migrated with zein,

The maize (Zea mays L.) floury-2 (fl2) mutation is associated with a general decrease in storage protein synthesis, altered protein body morphology, and the synthesis of a novel 24-kD alpha-zein storage protein. Unlike storage proteins in normal kernels and the majority of storage proteins in fl2

Opaque or nonvitreous phenotypes relate to the seed architecture of maize (Zea mays) and are linked to loci that control the accumulation and proper deposition of storage proteins, called zeins, into specialized organelles in the endosperm, called protein bodies. However, in the absence of null

Defective endosperm* (De*)-B30 is a dominant maize (Zea mays) mutation that depresses zein synthesis in the developing endosperm. The mutant kernels have an opaque, starchy phenotype, malformed zein protein bodies, and highly increased levels of binding protein and other chaperone proteins in the

Zeins, the major endosperm proteins in maize (Zea mays L.), are deficient in the essential amino acids lysine and tryptophan. Some mutant genes, like opaque-2 (o2) and floury-2 (fl2), reduce the levels of A- and B-zeins, thereby improving maize's nutritional value. Other mutants, such as

The sulfur-amino-acid-rich delta-zeins of maize ( Zea mays L.) are represented by 18-kDa and 10-kDa proteins. We have cloned a novel 11-kDa methionine-rich delta-zein from developing endosperm of the inbred line W23a1. The nucleotide sequence of this new delta-zein is identical to the published

The soft, starchy endosperm of the maize (Zea mays L.) floury 2 mutant is associated with a reduction in zein mRNA and protein synthesis, unique protein body morphology, and enhanced levels of a 70 kDa protein, that has been shown to be the maize homolog of a chaperonin found in the endoplasmic