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Title: (Starch synthesis in the maize endosperm as affected by starch synthesizing mutants)

Technical Report ·
OSTI ID:5859904

A recent findings is that the activity of the solubilized starch granule-bound enzyme is enhanced by the addition of Glc-1,6-bisP to a reaction mixture containing Glc-1-P as a substrate. The addition of F-1,6-bisP is nearly as effective as that of Glc-1,6-bisP while F-1-P, F-6-P, R-1-P, R-5-P, Ru-1,5-bisP, or Maltose-1-P are ineffective. It is a tenable hypothesis at the present time that Glc-1,6-bisP is also utilized as a substrate by the oligosaccharide synthase or another enzyme associated with it in the high molecular complex which contains the oligosaccharide synthase that has been freed from the starch granules by the procedure of MacDonald and Preiss. This fraction also appears to be capable of interconverting Glc-1,6-bisP and F-1,6-bisP and this can account for the observation that F-1,6-bisP has the ability to accelerate the incorporation of Glc-1-P into oligosaccharides as does Glc-1,6-bisP. They are attempting currently to test the possibility that Glc-1,6-P is utilized to some extent as a substrate and that the PO{sub 4} present on C6 in some Glc moieties in the oligosaccharide chains derives from this source.

Research Organization:
Wisconsin Univ., Madison, WI (USA). Lab. of Genetics
Sponsoring Organization:
USDOE; USDOE, Washington, DC (USA)
DOE Contract Number:
AC02-82ER12031
OSTI ID:
5859904
Report Number(s):
DOE/ER/12031-T3; ON: DE91010194
Country of Publication:
United States
Language:
English