Developmentally dependent expression of tissue specific amylases in maize

  title={Developmentally dependent expression of tissue specific amylases in maize},
  author={Su En Chao and J. G. Scandalios},
  journal={Molecular and General Genetics MGG},
SummaryIncrease of amylase activity and qualitative changes of the array of amylase isozymes as a function of the maize seedling age and tissues were studied. About 80% of the amylase was located in the endosperm and scutellum and the remaining 20% in the shoot and root throughout the first 12 days of sporophytic development. When the total amylase peaked at the 8th day of germination, the endosperm contained 3–5 times more amylase than did the scutellum. The major increase in amylolytic… 

Structural and regulatory differences in amylase isoenzymes in germinating Brazilian barley cultivars

The results indicate that regulatory polymorphism is the principal agent responsible for amylase variability in the barley varieties analyzed.

Cotyledons of Pea (Pisum sativum L.) Seedlings1

The most abundant a-amylase (EC in shoots and cotyledons from pea (Pisum sativum L.) seedlings was purified 6700and 850-fold, respectively, utilizing affinity (amylose and cycloheptaamylose)

Wide hybridization between Brazilian soybean cultivars and wild perennial relatives

Morphological, cytological and isoenzyme patterns confirmed the hybrid status of all seven mature plants, all of which were generated using G. tomentella G 9943 as the paternal parent, and it was observed that all soybean lines crossed with G9943 were capable of producing mature hybrid plants.

Isoenzyme variation in the leaf-cutting ants Acromyrmex heyeri and Acromyrmex striatus (Hymenoptera, formicidae)

This is the first study of isoenzyme variability in the leaf-cutting ants (Myrmicinae, Attini) Acromyrmex heyeri and A. striatus which are common throughout the southern Brazilian state of Rio Grande do Sul.


Genetic variability within and among different samples of peanut (Arachis hypogaea L.) from the cultivars Roxo, Tatu Branco, Tatu Vermelho, Tatuí Vermelho and Tatuí (white skin seeds) was evaluated



Alpha-amylase of maize: differential allelic expression at the Amy-1 gene locus, and some physiochemical properties of the isozymes.

ULTIPLE molecular forms (isozymes) of amylase have been reported in barley tobacco crown-gall tissue culture , rice maize Much of the earlier work on amylases has dealt with possible physiological

Enzymic Mechanism of Starch Breakdown in Germinating Rice Seeds: III. alpha-Amylase Isozymes.

Nearly identical patterns of amylase isozyme bands on a polyacrylamide gel disc electrophoresis in combination with isoelectric focusing indicate the intrinsic role of gibberellic acid in the starch breakdown in germinating rice seeds.

Immunochemical study of changes in the soluble proteins of wheat during germination

During germination and early growth the general immuno-electrophoretic pattern of soluble proteins of two wheat species showed similar changes, but the antigenic α-amylase of germinated seeds was shown to be absent from the mature seeds, even as an inactive-form.

Identification and genetic control of starch-degrading enzymes in maize endosperm

Results of genetic crosses with respect to zone 2 amylase show that it is controlled by a pair of alleles (Amy-2A and Amy-2B) acting without dominance, and it further appears that Amy- 2 and Ct (catalase) are linked with 5% recombination frequency.

Enzymic mechanism of starch breakdown in germinating rice seeds : 12. Biosynthesis of alpha-amylase in relation to protein glycosylation.

Results indicate that heterogeneity of alpha-amylase isozymes is not due to glycosylation of the enzyme protein but likely to differences in the primary structure of the protein moiety, which altogether support that rice alpha-AMylase Isozymes are encoded by multiple genes.


  • J. VarnerG. R. Chandra
  • Medicine, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1964
The glycogen-a-amylase complex was incubated at 250 for 1 hr to digest the glycogen then dialyzed overnight against 0.01 M L-threonine and after 10 min the precipitate recovered by centrifugation.

A test for de novo synthesis of enzymes: density labeling with H2O18 of barley alpha-amylase induced by gibberellic acid.

  • P. FilnerJ. Varner
  • Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1967
aleurone of nate fractions were collected directly into 5.0 ml of Bray's solution for scintillation counting. The other set of fractions was used for enzyme or chemical assays. In addition, the